Biochem HND - 0

NATIONAL BOARD FOR TECHNCIAL EDUCATION
KADUNA
HIGHER NATIONAL DIPLOMA
IN
BIOCHEMISTRY
CURRICULUM AND COURSE SPECIFICATIONS
2003
PLOT ‘B’ BIDA ROAD, P.M.B. 2239, KADUNA-NIGERIA

HIGHER NATIONAL DIPLOMA IN BIOCHEMISTRY
GENERAL INFORMATION
PROGRAMME GOAL:
This programme is designed to produce biochemical technologist capable of applying laboratory techniques to complement the work
of scientist in industrial and laboratory biochemical analysis and production processes.
PROGRAMME OBJECTIVES:
A diplomate of this programme should be able to:
Carry out biochemical analysis in laboratories in education, food and chemical industries and in research institutes.
STRUCTURE OF THE PROGRAMME:
NATIONAL DIPLOMA (ND)

The National Diploma in food Technology is a terminal programme and is structured to last for two years (four semesters). This
incorporates three to four months of supervised industrial attachment at the end of the first year or the first two semesters of the
programme.
HIGHER NATIONAL DIPLOMA

The Higher National Diploma Biochemistry programme is terminal and is structured to last for two years (four Semester). This
incorporates four to six months of supervised industrial attachment.
CURRICULUM
Curriculum of all programmes consists of four main components. These are:
i. General studies/Education
ii. Foundation courses
iii. Professional courses
iv. Student Industrial Work Experience scheme (SIWES).
The General Education component shall include courses in Art and Humanities- English Language, Communication, History. These
are compulsory.
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Mathematics and Sciences (for non-science based programmes)
Social studies-Citizenship (the Nigerian Constitution) political science, Sociology, Philosophy, Geography, Entrepreneurship
Physical and Health Education (one semester credit only).
Foundation Courses include courses in Economics, Mathematics, Pure Sciences, Technical drawing, descriptive geometry, Statistics,
e.t.c. The number of hours will vary with the programme and may account for about 10-15% of total contact hours. Professional
courses are courses which give the student the theory and practical skills he needs to practice his field of calling at the theory and
practical skills he needs to practice his field of calling at the technician /technologist level. These may account for between 60-70% of
the contact hours depending on programme.
Student Industrial Work Experience Scheme (SIWES) shall be taken during the long vacation following the end of the second
semester of the first year. See de tails of SIWES in Guideline on SIWES at page 5.
CURRICULUM STRUCTURE
ND Programme
The structure of the ND Programme consists of four semesters of classroom, laboratory and workshop activities in the college–and a
semester (3-4 months) of supervised industrial work experience scheme (SIWES). Each Semester shall be of 17 weeks duration made
up as follows:
15 contact weeks of teaching, i.e. recitation, practical exercises, quizzes, test e.t.c; and a 2 weeks SIWES shall take place at the end of
the second semester of the first year.
HND Programme
The Higher National Diploma Biochemistry programme is a terminal programme and is structured to last for two years (four
semesters). This incorporates four to six months of student industrial attachment.
ACCREDITATION:
Each programme offered either at the ND or HND level shall be accredited by NBTE before the diplomates can be awarded either of
the two diploma certificate. Details about the process of accreditation a programme for the award of the ND or HND are available for
the executive secretary, Programmes Division, National Board for Technical Education, Plot B, Bida Road, P.M.B. 2239, Kaduna,
Nigeria.
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CONDITIONS FOR THE AWARD OF THE ND/HND
Institutions offering accredited programmes will award the Nation Diploma to candidates who successfully completed the programme
after passing prescribed coursework, examinations, diploma project and the supervised industrial work experience. Such candidates
should have completed a minimum of between 72 and 80 semester credit units depending on the programme. Diplomates shall be
classified as follows:
Distinction - GPA of 3.50 and above
Upper Credit -GPA of 3.00 - 3.49
Lower Credit -GPA of 2.50 – 2.49
Pass - GPA of 2.00 – 2.49
Fail - GPA of below 2.0
EVALUATION OF AWARD:
All terminals National Diploma and Higher National Diploma examinations must be externally moderated in grading the award, the
Board’s unified Grading system should be applied.
GUIDANCE NOTE FOR TEACHERS TEACHING THE PROGRAMME

The new curriculum is drawn in unit courses. This is in keeping with the provisions of the National Policy on Education which stress
the need to introduce the semester credit which will enable a student who so wish to transfer the units already completed in an
institution of similar standard from which he is transferring.
In designing the units the principle of the modular system by product has been adopted; thus making each of the professional modules,
when completed provides the student with technician operative skills, which can be use d for employment purposes.
As the success of the credit unit system depends on the articulation of programmes between the institutions and industry, the
curriculum content has being written in behavioral objectives, so that it is clear to all the expected performance of the student who
successfully completed some of the courses or the diplomates of the programme. There is a slight departure in the presentation of the
performance based curriculum which requires the conditions under which the performance are expected to be carried out and criteria
for the acceptable levels of performance. It is a deliberate attempt to further involve the staff of the department teaching the
programme to write their own curriculum stating the conditions existing in their institution under which the performance can take
place and to follow that which the criteria for determining an acceptable levels of performance. Departmental submission on the final
curriculum may be vetted by the Academic Board of the institution.
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Our aim is to continue to see to it that a solid internal evaluation system exists in each institution for ensuring minimum standard and
quality of education in the programmes offered through the polytechnic system.
The teaching of the theory and practical work should, as much as possible, be integrated. Practical exercises, especially those in the
professional courses and laboratory work should not be taught in isolation from the theory. For each course, there should be balance of
theory to practice in the ratio of 50:50 or 60:40 or the reverse.
GUIDANCE FOR THE SIWES PROGRAMME

For the smooth operation of the SIWES the following guidelines should apply:
Responsibility for Placement of Students

Institutions offering the ND programme shall arrange to place the students in industry. By April 30 of each year, six copies of the
master list showing where each student has being placed shall be submitted to the executive secretary, NBTE which shall, in
return, authenticate the list and forward it to the industrial Training Fund Jos.
The Placement Officer should discuss and agree with industry on the following:
i. A task inventory of what the students should be expected to experience during the period of attachment. It may be wise to
adopt the one already approved for each field.
ii. The industry-based supervisor of the student during the period likewise the institution based supervisor.
iii. The evaluation of the student during the period. It should be noted that the final grading of the student during the period of
attachment should be weighted more on the evaluation by his industry-based supervisor.
Evaluation of Students during the SIWES

In the evaluation of students, cognizance should be taken of the following items:
a) Punctuality
b) Attendance
c) General Attitude to work
d) Respect for authority
e) Interest in the field/technical area
f) Technical competence as a potential technician in his field.
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GRADING OF SIWES
To ensure uniformity of grading scales, the institution should ensure that the uniform grading of students work which has been agree
to by all polytechnics is adopted.
THE INSTITUTION BASED SUPERVISOR

The institution based supervisor should initiate the log book during each visit. This will enable him to check and determine to what
extent the objectives of the scheme are being met and to assist students having any problems regarding the specific assignments given
to them by industry-based supervisor.
FREQUENCY OF VISIT
Institution should ensure that students placed on attachment are visited within one month of their placement. Other visits shall be
arranged so that
There is another visit six weeks after the first visits; and
A final visit in the last month of the attachment.
STIPEND FOR STUDENTSS IN SIWES

The rate of stipend payable shall be determined from time to time by the Federal Government after due consultation, with the Federal
Ministry of education, the Industrial Training Fund and the NBTE.
SIWES as a Component of the Curriculum

The completion of SIWES is important in the final determination of whether the student is successful in the programme or not. Failure
in the SIWES is an indication that the student has not shown sufficient interest in the field or has no potential to become a skilled
technician in his field. The SIWES should be graded on a fail or pass basis. Where a student has satisfied all other requirements but
failed SIWES, he may only be allowed to repeat another four months SIWES at his own expense.
National Board for Technical Education,

Kaduna.
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COURSE COURSE TITLE L T P CU CH PRE-REQUISITE
CODE
COM 301 Computer Application 1 - 2 2.0 30
STH 311 Biochemical Methods I 2 - 2 3.0 65
STH 312 Physical Biochemistry I 1 - 2 2.0 45
STH 313 Microbial immunochemistry 2 - 2 3.0 60
GLT 303 Biological and Chemical Instrumentation 2 - 3 3.0 75
GLT 301 Laboratory Management 2 - - 2.0 30
GNS 301 Use of English 2 - - 2.0 30
12 - 14 18 375
GLT Course see General Laboratory Techniques syllabus

GNS Course see General Studies syllabuses
STH 424 See Page 68 in Science Lab. Technology syllabus
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HND BIOCHEMISTRY
1ST YEAR
CODE
STA 305 Biometrics 2 - 2 3.0 60
STH 321 Biochemical Method II 2 - 3 3.0 75
STH 322 Intermediary Metabolism I 2 - 2 3.0 60
STH 323 Regulation of Cell Metabolism 1 - 2 3.0 60
STH 324 Nutritional Biochemistry II 1 - 3 2.0 60
STH 325 Physical Biochemistry II 2 - 2 2.0 45
GLT 302 Instrumentation (General) 2 - 2 3.0 60
GNS 302 Communication in English 2 - 2 2.0 30
12 - 12 21 450
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HND BIOCHEMISTRY
2ND YEAR

CODE
STH 411 Intermediary Metabolism II 1 - 2 2.0 30
STH 412 Nutritional Biochemistry II 1 - 3 2.0 60
EDP 413 Entrepreneurship Development 2 - - 2.0 30
STH 413 Biotechnology and Genetic Engineering 2 - 2 3.0 60
STH 414 Seminar - 1 2 2.0 30
GNS 401 Literacy Appreciation and Oral Composition 2 - 6 2.0 90
8 1 15 11 300
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HND BIOCHEMISTRY
2ND YEAR

CODE
STH 421 Tissue Biochemistry 2 - 2 3.0 60
STH 422 Forensic Biochemistry 1 - 2 2.0 45
STH 423 Industrial Biochemistry 2 - 3 3.0 60
STH 424 Comparative Biochemistry 2 - 2 3.0 60
STH 425 Seminar - - - 1.0 -
STH 426 Project - - - 4.0 -
7 - 9 20.0 225
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PROGRAMME: BIOCHEMISTRY (HND)
COURSE: BIOCHEMICAL METHOD I
CODE: STH 311
DURATION: 60Hours, 15weeks, (2Hours Lecture, Tutorials 0.2 Hours Practicals
UNIT: 3.0
GOAL: This course is designed to enable the diplomate carry out various analytical method
in Biochemistry.
GENERAL OBJECTIVES:
On completion of this course, the student should be able to:
1.0 know the general principles of biochemical investigation.
2.0 Know the various principles and application of configuration.
3.0 Understand the principle and application of dialysis.
4.0 Understand the principle and application of manometric techniques.
5.0 Understand the principle and application of polarimetry.
6.0 Understand the principle of refractometry techniques.
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PROGRAMME: HND BIOCHEMISTRY
Course: BIOCHEMICAL METHODS I Course Code: STH 311 Contact Hours 60 Hrs 2-0-2
Course Goal: This course is designed to enable the student carry out various analytical method in biochemistry
WEEK General Objectives 1.0 Know the general Principles of biochemical investigation
Special Learning Objective: Teaching Activities Resources
Explain the fundamental concepts and approaches Lectures High speed centrifuge
1-2 which has to be considered when designing
biochemical experiments.
Describe the methods for isolation of particles or Laboratory experiment in cell “
organelles inside a cell . isolation
Organelle/particle components are separated from “ “
each other by various separation techniques.
Extract various organelles from the cell by
centrifugation technique. Laboratory practical in “
Describe the qualitative and quantitative analytical centrifugation of the cell
techniques that are employed in the Lecture Teaching tools
determination of the components of the cell.
Describe the Spectroscopic techniques which are
available for the study of the components at Lecture “
atomic or molecular level.
Describe the various combination of analytical
techniques available for the elucidation of the Lecture “
mode of action and inter-relationships of
components within particles and cells.
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General Objectives : 2.0 Know the various principle
and application of centrifugation.
WEEK Special Learning Objective: Teachers Activities Resources
3-5 2.1 Define Centrifugation Lecture Teaching tools

2.2 Describe the various principles
Of Centrifugation “
2.3 Explain the applications of centrifugation as
a Separation techniques.
2.4 List the parameters which determine the “ “
Sedimentation rate (inversely related to time taken).
2.5 . List the parameters which determine the successful
separation of mixture of heterogenous particles.
2.6 Explain the importance of the density and viscosity
of the medium in facilitating the separation. “
2.7 List the order of sedimentation of the major cell “
components.
2.8 Define preparative centrifugation and analytical
centrifugation and state the difference(s) between the
two. “
2.9 List the applications of preparative and analytical
centrifugation. “
2.10 List the three major classes of preparative
centrifugation (general purpose centrifuge, higher
speed centrifugation and the preparative
ultracentrifuge) their rotor designs and uses).
2.11 Describe the different methods of preparative “ “
centrifugation viz:
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i) Differential centrifugation
ii) Rate-Zonal centrifugation.
iii) Isopyenic (equal-density) centrifugation
iv) Equilibrum Isodentsity centrifugation
2.12. Identify the types of media for the preparation of
liquid density gradients.
2.13. Explain the discontmous or layering density
gradient techniques.
2.14. Explain the continuous density gradient techniques
2.15. Describe how gradients are removed from
centrifuge tubes.
2.16. Carry out differential centrifugation and present the High speed centrifuge
results.
2.17. Describe the basic principles of the analytical
ultracentrifugation.
2.18. Apply analytical ultracentrifugation method in the l
i)Determination of molecular weights
ii) Estimation of purity of macromolecules. Ultracentrifuge
iii) Detection of conformational changes in
macromolecules.
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WEEK General Objectives 3,0 Understand the Principle and Application of Dialysis
Special Learning Objective: Teachers Activities Resources
6-7 3.1 Explain the term “dialysis” Lecture

3.2 Describe the need for dialysis during protein Laboratory Demonstrate the
purification. analysis experiment
3.3 Apply the process of dialysis/ultradialysis protein
purification. Lecture
3.4 Explain the irritation of dialysis.
3.5 State the steps that can be taken to ensure successful “
dialysis of a protein solution.
3.6 List the applications of dialysis. “
WEEK General Objectives 4.0 Understand the Principles and Application of Manometric Techniques.
8-9 4.1 Explain the term “Manometry” Show and describe the Manometer
4.2 4.2 Explain the principle and application of manometer to students
Manometric Technique. “ “
4.3 Explain the Similarities and differences between
Manometric and the oxygen electrode. “
4.4 Define the terms Respiratory Quotent and Metabolic
Quotent. “ “
4.5 Explain the three types of Manometry viz:
i) Constant volume Manometry. “
ii) Constant Pressure Manometry.
iii) Differential Manometry. “
4.6 Describe the operation, and principle and calibration
of the Warburg constant volume Manometre. Show and describe the
4.7 Describe the Gilson Differential Respirometre. respirometer to students Respirometer
4.8 List the general procedure for the operation of a
Manometre. “
4.9 List the application of manometry. “
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WEEK General Objectives 5.0 Understand the Principles and Applications of Polarimetry.
10-12 5.1 Explain the term “plane polarized light” Show and describe the Polarimeter
5.2 List and identify the substances that produce plane- polarimeter to students
polarized light e.g Nicol Prism, tourmaline, ice/spa. “
5.3 Explain the term “Optical activity”. “ “
5.4 List the substances possessing optical activity (e.g. “
simple sugars). “
5.5 Distinguish between optically active compounds as Laboratory experiment of
dextro and laera rotaroty. optical action compounds using
5.6 Explain the specific rotation of a compound. polarimeter
5.7 Describe the components of a polarimetre; Light
source, polarizer tube analyzer. Lecture “
5.8 Describe the method of determination of specific
rotation of a substance.
5.9 Calculate the concentration and specific rotation of a “
substance. “
5.10Explain the limitation of a polarimeter in analytical
work “
5.11Determine the specific rotation of given simple “
sugars using polarimerer. Laboratory experiment of
5.12Interpret the results obtained in 5.11 above. optical action compounds using
5.13 Identify compounds tentatively using the result in polarimeter
5.12 above.
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WEEK General Objectives 6.0 Understand the principle of Refractometry techniques.
13-14 6.1 Define “critical angle” and “refractive index” of a Show and describe the Refractometer
substance. refractometer to students
6.2 Describe the method of determining the refractive “
index of a substance. “
6.3 Describe a typical refractometre e.g abbe
refractometre. “ “
6.4 Represent the refractometre diagrammatically.
6.5 Describe the operation of the refractometre. “
6.6 List the applications of a refractometre in analytical “ “
work e.g. determination of the purity of a substance. “ Abbe retractometer
6.7 Determine the refractive index of a solution wing Students to determine “
Abbe refractiometer. refractive index
6.8 State the limitations of the refractometre in analytical Abbe retractometer
work.
6.9 Analyse a lipid using a refractometer. Students to analyse lipids using
refractometer
“
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PRACTICAL CONTENTS
WEEK PRACTICALS TEACHERS ACTIVITIES RESKOURCES

1-2 1.4 Extract various organelles Guide students on laboratory High speed centrifuge sample of
from the cell by centrifugation experiment on various cell cell organ
techniques organs using centrifugation
methods
2.2 Identify the type of media for Show students on how to identify
the preparation of liquid density liquid density gradients and its High speed centrifuge cell
graduates preparation in the laboratory. sample
2.6 Carry out different
centrifugation and present the Carry out laboratory practical on High speed centrifuge
results different centrifuge with high
2.18 Apply analytical speed.
ultracentrifugation in the
determination of
Carry out laboratory Ultracentrifuge
Molecular weights ultracentrifugation to determine
Estimation of purity of molecular weight of
macromolecules macromolecules.
Detection of conformation
changes in
macromolecules
3.9 Prepare buffers for biochemical Guide students to prepare buffer Salt and acid for buffer
experiments for biochemical experiment preparation
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10-12 5.8 Analyse the method of Carry laboratory experiment of Polarimeter
determination of specific rotation of optical compounds polarimeter.
a substance
5.11 Determine the specific rotation Carry compounds using
of a given sample sugar using polarimeter Pollarimeter
polarimeter.
Interpret the results obtain in 5.11

Identify compounds tentatively
using the result in 5.11
6.2 Analyse the method of

determining the refraction index
of a substance Guide students to determine the Refract meter refractive pin
refractive index of any given
substance
6.7 Determine the refractive index
of a solution using
6.9 Analyse a lipcal using a Guide students to determine Refract meter
refractive meter refractive index of a wing
solution
Guide students to analyse lip cal Abbe refmetometer

using refract meter
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COURSE: PHYSICAL BIOCHEMICAL I
CODE: STH 312
DURATION: 45Hours/15Weeks/(1Hour Lectures,Tutorial 0, 2Hours Practicals)
UNIT: 2.0
GOAL: This course is designed to provide the student with a basic knowledge
of physical biochemistry.
GENERAL OBJECTIVES: 1.0 Understand the properties of water,solutions and colloids
2.0 Understand the concepts of Acids Bases and Salts.
3.0 Understand the relevance pH and buffer system in biochemical reaction
4.0 Understand the Application of Acid –Base fluid and electrolyte control to some biochemical
processes
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Course: PHYSCIAL BIOCHEMICAL . I Course Code: STH 312 Contact Hours 45 Hours 1-0-2
Course Goals: This course is designed to provide the student with a basic knowledge of physical Biochemistry
WEEK General Objectives 1.0 Understand the properties of water, solutions and colloids
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1-3 1.1 Describe the structure and properties of water Lecture Chalkboard
e.g. SHC, Heat of vaporation., latent Heat etc.
1.2 Describe the electronic structure of water “
molecule and the implications of each property
e.g. polarity hydrogen-bonding, surface tension.
1.3 Explain some proposed models for the structure “
of ice and liquid water.
1.4 Describe some physiochemical properties of “
water and how they are particularly suited to the
role of water as the solvent of biological systems.
1.5 Demonstrate the solubility of water in Practicals Demonstration Practicals
comparism to other solvents like acetone
benzene, alcohol, etc.
1.6 Explain surface tension it’s 51 units of Lecture
qualification.
1.7 Describe the phenomenon of surface tension and “
the biophysical implication of surface tension.
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WEEK General Objectives
Special Learning Objective: Teachers Resources
Activities
1.8 Determine surface tension by capillarity. Lecture Capillary tube
1.9 Explain and compare the properties of solution,
colloidal dispersed parties, suspension in terms of “
average diameter of dispersed particles, behaviour
towards gravity and light filteravability, homogeneity “
and number of phases present
1.10Prepare different types of solutions Practical preparation of Glasswares
1.11Describe the different types of solutions and their solutions
common examples.
1.12Explain the quantitative expressions of concentration “
– molar concentration, concentrations expressed as “
percentage weight/volume; volume/volume,
weight/weight milligram percentage part per million
and parts per billion.
1.13Carry out calculations involving 1.9 above.
1.14 Prepare dilute solutions from more concentrated Different types of salts,
solutions. “ concentrate acids and bases.
1.15Explain the colligative properties of non electrolyte Glassware
solutions viz. Lectures
Result’s law and the lowering of vapour
pressure.
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Special Learning Objective: Teachers/Learning Activities Resources
(b) The relation between boiling point
elevation and the molarity of the solution
(c) Relation between freezing point
depression and morality of a solution
(d) Simple calculations based on (a) – (c)
above and their applications
(e) The phenomenon of osmotic pressure and
the reaction between osmotic pressure
and the molecular weight of solute.
(f) The importance of osmotic phenomenon
on biological system.
1.16 Determine the effects of 1.15 (b) (c) & (e) above on Lecture Practical – Osmotic pressure
What? determination apparatus
1.17 Determine osmotic pressure of a solute “ Practicals
1.18 Explain the term Electrolyte solution and “
(i) Salting in and Salting out effects
(ii) The Donnan Effect
(iii) Dialysis
(iv) Applications of (i) – (iii)
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WEEK General Objectives 2.0 Understand the Concept of Acids, Bases and Salts
4-5 Special Learning Objective: Teachers Activities Resources
2.1 Understand the concepts of acids, bases and salts Lecture PH meter
viz.
Bronsted-lowry acids and bases , alkalis,
ampholytes; strength of acids and bases.
Hydrogenion concentration and pH: Definition of
PH.
(b) Derivation of KW (ionic product of water).
(c) Temperature and Kw and its biological
implication
2.2 Measure pH using pH meter lovibond comparator Carry out practicals on pH meter PH meter
2.3 Explain the principle of the pH meter: glass and “
Calomel electrodes.
2.4 Explain the theory and practice of pH of strong acids “
2.5 Explain the concept of dissociation of Acids and “ Practical
bases viz. Burrette, pipette Beakers,
(a) Strong acids and calculation of pH of Cornical flasks.
strong acids
(b) Weak acids: the Henderson – Hasselbalch
equation
(c) Titraction curves: Strong acid/strong
base; weak acid/strong base; tiraction
curves of polyprotic acids.
2.6 Explain the common ion effect and its relationship to Lecture
such biochemical phenomena as Urinary calculus,
bile stones and gout.
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WEEK General Objectives 3.0 Understand the Relevance of pH and Buffer Systems in Biochemical Reactions
6-7 3.1 Explain the terms: Lecture Making of Teaching
(a) Buffering range of a very weak acid and tools
(b) Buffering capacity
3.2 Explain the properties of cytoplasmic constituents “ “
(acidic, basic and amphoteric) e.g. Aminoacids,
protein; heamoglobin etc.) which contribute to the
buffering ability of cellular contents. “
3.3 Explain the importance of bicar bonate buffer Hcoz-: “
H2Co3 in the buffer system of the entire organism. “
3.4 Explain the nature of the buffering systems in the “
blood (proteins, Heamoglobin, phosphate and
bicarbonate). “
3.5 State the normal intracellular and extracellular fluid “
pH value of plants and animals (pH 7.4)
3.6 Explain why the pH of intracellular fluids differ “ “
widely on their values (gastric juice – 1.5; intestinal
content – 6).
3.7 Explain why attainment of an optical pH is essential
for microbial function and growth
3.8 List types of buffer systems used in biochemical
Work.
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3.9 Prepare buffers for biochemical experiments Practical Salts and acids for buffer
3.10 Calculate the pH of buffers “ preparation,
3.11 Determine the pH of colorless and colored fluid of “ glass ware
biological origin using organic indicators and pH pH meter
meter.
“
WEEK General Objectives 4.0 Understand the Application of Acid-Base Fluid and Electrolyte control to some Biochemical
Processes
4.1 Identify the metabolic products that can effect Lecture Teaching tools
8-9 body fluid pH
4.2 Explain the role of blood buffers in pH control “ “
4.3 Explain the respiratory control of blood pH via “
hypo and hyper – ventilation, and isohydric “
carriage of carbon dioxide
4.4 Explain the limitation of respiratory control of pH “ “
4.5 Compare the rate and depth of pH compensation “ “
by respiratory control with those of renal control.
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PRACTICAL CONTENTS
WEEK PRACTICAL TEACHERS ACTISITIES RESOURCES

1-3 1.9 Analyse and compare the properties of Guide students on practical preparation Glass wares
solution colloidal dispersed particles, of solutions
suspension of average diameter of dispersed
particles behavior towards gravity and light
tilteravability, homogeneity and number of
phases present
Guide students on practical preparation Glass wares
1.10 Prepare different types of solutions of defferent solutions
-calculations
1.13 Carry out calculations involving (1.9
above) Prepare students to dilute solutions from
more concentrated solutions
1.14 Prepare defuse solutions from more Guide students to determine different
concentrated solutions type of osmotic pressure of a solute salt
diluted water, bases glass ware
1.19Determine osmotic pressure of a solute
2.3 Measure pH using pH meter lovibond Carry out practicals on pH meter pH meter
comparator
6-7 Prepare buffers for biochemical experiments Guide students to prepare buffer for Salt and acid for buffer
biochemical experiments. preparation
3.11 Determine the pH of colorless and Glass ware
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colored fluid of biological origin using Carry out practicals to determine the pH Ph meter
organic indicator and pH meter of colorless and colored fluids of
biological origin
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COURSE: MICROBIAL IMMUNOCHEMISTRY
CODE: STH 313
DURATION: 60 Hours/15Weeks (2Hours Lecture/Tutorial 0, 2Hours Practicals)
UNIT: 3.0
GOAL: This course is designed to provide the student with a knowledge of the chemical
Nature of microbial immune system
GENERAL OBJECTIVES: On completion of this course,the student should be able to:
1.0 Understand the molecular structure of microorganism
2.0 Understand the general payments for microbial growth and various method
of measuring microbial growth.
3.0 Understand the various source of Nitrogen,Carbon, and energy to microorganism
and the effect of various concentrations of the different carbon sources on growth
4.0 Understand the nature of the immune system and compliment fixation.
5.0 Understand antigen- antibody and the significance of immunology on public health.
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Course: MICROBIAL IMMUNOCHEMISTRY Course Code: STH 313 Contact Hours 60 hrs 2-0-2
Goal: This course is designed to provide the students knowledge of the chemical nature of microbial immune systems
WEEK General Objectives 1.0 Understand the Molecular structure of microorganisms
1.1 Explain the various methods of microbial cell Explain using some specific
disruption e.g. solid and liquid shear methods examples.
etc.
1.2 Explain the separation of the components of Microscope cell tissue.
disrupted cells. Demonstrate experiment on cell
1.3 Describe the surface appendages of the bacterial separation techniques.
cell e.g. flagella, capsule, etc.
1.4 Describe the cell wall components of gram
negative and gram positive bacteria.
1.5 Carry out the following stemming techniques: Supervise individual gram Microscope.
gram stain, spore stain, flagella stain. staining of a bacteria etc. and
1.6 Describe the structure of cell membrane. grade reports.
1.7 Describe the structure and components of Use A/V facilities. Overhead projectors
cytoplasm. Explain the component using Microscopes.
film strides.
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WEEK General Objectives 2.0 Understand the general requirements for microbial growth and the various methods of
Measuring microbial growth.
10 - 12 2.1 Explain the concept of microbial growth as being Demonstration using projectors. Audio visual facilities
increase in population /cell, number/cell mass rather
than increase in size or individual.
2.2 Describe the general requirements for microbial “
growth.
2.3 Describe the influence of environmental factors on use examples such as slow growth Microscopes Colony
growth of micro organisms. under refrigeration. counters
2.4 Demonstrate the effects of some of the factor in 2.2 Laboratory Practical on growth of
and 2.3 above on microbial growth. microbes.
2.5 Measure microbial growth directly. Practical on monitoring growth of
2.6 Measuring microbial growth center. Directly/indirectly.
2.7 Describe the microbial growth curve. Drawings and overhead projector of
2.8 Explain the mathematics of microbial growth. microbial growth curve.
32
General Objectives:3.0 Understand the various sources of nitrogen, carbon and energy to microorganisms, and the
WEEK effect of various concentrations of the different carbon sources on growth.
13 - 14 3.1 Explain the importance of nitrogen sources in Classroom lecture and
microbial growth. demonstration.
3.2 List inorganic sources of nitrogen. “
3.3 3.3 List organic sources of nitrogen. “
3.4 Classify microorganisms according to mode of “
nitrogen (e.g. organotroph and litotroph). “
3.5 Explain monosaccharides as sources of carbon and “
energy. “
3.6 Explain oligosaccharides as sources of carbon and “
energy.
3.7 Explain polysaccharides as sources of carbon and
energy. “
3.8 Explain derivatives of the various carbohydrates as “
sources of carbon and energy. “
3.9 Explain derivatives of the various carbohydrates as
sources of carbon and energy.
33
WEEK General Objectives 4.0 Understand the nature of the immune system and complement fixation.
4.1 Outline the early concepts of immunology and public Give examples.
13-14 health.
4.2 Explain the terms antigen, antibody and other Lectures
components of the immune system.
4.3 Explain the structure and synthesis of antibodies. Lectures.
4.4 Explain the terms natural and artificial immunity. Lectures.
4.5 Explain the term complement.
4.6 Prepare and standardize complement.
4.7 Prepare and standardize hemolytic. Conduct practical Glasswares reagents.
4.8 Prepare an indicator system. “
4.9 Carry out complement-fixation proper. “
34
WEEK General Objectives 5.0 Understand antigen-antibody and the significance of immunology on public health.

5.1 Explain the various antigen-antibody reactions. List common examples
5.2 Explain the various types of hypersensitivity Use audio visuals
(delayed, immediate etc.) and allergic reactions.
5.3 Describe the factors affecting antigen-antibody Lecture
reactions.
5.4 Explain the A,B,O Blood grouping (blood and “
serum).
5.5 Explain the rhesus factor and blood and rhesus Show examples
incompatibilities.
5.6 Carry out any of the following reactions; Conduct practical, on agglutination,
Agglutination, precipitation etc. Precipitation
5.7 Explain the mechanism of resistance to infection. Lecture
5.8 Explain the relationship of infection to immunity. “
5.9 Explain the interaction of drugs to the immune Describe examples.
system.
5.10List common communicable diseases in Nigeria e.g. Use charts and films and slides. Overhead projector
Cholera, AIDS, etc.
5.11Explain the immune measures against the diseases in
5.10 above.
5.12Distinguish between epidemics, endemics and pan Field mp’
emics etc.
5.13Explain the control and preventive methods “
applicable to each situation in 5.12 above.
35
PRACTICAL CONTENTS
WEEK PRACTICAL STEACHERS ACTIVITIES RESOURCES

1-8 1.2 Analyse the separation of the components of Demonstrate experiments on Microscope, cell tissue
disrupted cells cell separation techniques
1.5 Carry out the following stemming techniques Supervise students on staining Microscope
gram slain, spone Stan flagella stain techniques
13-14 4.6 Prepare and standardize complement Conduct practical on Glass wares
4.7 Prepare a standardize hemolytic standardize complement Reagents
4.8 Prepare an indicator system Conduct practical on Reagents
standardize hemolytic
Conduct practical on how to
prepare indicators
5.6 Carry out any of the following Conduct practical on Reagents

Feat ions, Agglutination, precipitation etc agglutination, precepitation BNlood sample
36
PROGRAMME: BIOCHEMISTRY HIGHER NATIONAL DIPLOMA
COURSE: REGULATION OF CELL METABOLISM
CODE: STH 323
DURATION: 60 Hours/15Weeks/Lecture = 2, Tutorials = 0 Practicals=3
UNIT: 3.0
GOAL: This course is designed to enable the diplomates with an understanding
Of the general principles in the regulation/control of biochemical reaction that
Occurs in the cell.
GENERAL OBJECTIVES; On completion of the course the diplomate should be able to:
1.0 Understand the concept of Homoeostasis
2.0 Understand the effect of the hormones on cellular metabolism.
3.0 Understand the mechanism of enzyme regulation/control
4.0 Understand the methods of PH fluid and electrolyte control in the body.
5.0 Understand the genetic factors that regulate the intracellular concentration of various proteins.
37
PROGRAMME : HND BIOCHEMISTRY
Course: Regulation of Cell Metabolism Course Code: STH 323 Contact Hours 60 Hours 2-0-2
Course Goal: The course is designed to enable the students with a clear understanding of the general principle in the
regulation/control of biochemical reaction that occurs in the cel
WEEK General Objectives : 1.0 Understand the concept of Homoeostasis
Homoeostasis
1-2 Explain the term homoeostasis. Demonstration and class Teaching tools
Distinguish between negative feedback and positive lectures and discussions “
feedback.
Describe a homeostatic control system. Illustrate and demonstrations “
38
2.1 Describe the constitution, types, body. Lectures Charts showing the major
2.2 Hormones endocrine glands and their
2.3.2 See P.84 – P.86. secretions.
2.3 Explain the role of the following substances in
plants: Charts showing the hormones
2.4 (a) auxins. involved in regulation of
(b) gibberellins. moulting in insect
(c) Kinetin metamorphosis.
(d) Ethylene
2.5 Differentiate between the role of vitamins and
hormones in growth. Glasswares and reagents.
2.6 Isolate and purify hormones and hormone like. Practical isolation and
Substances from different laboratory animals purification, students to work Using Callow’s original
and plants. individually. method.
2.7 Identify neutral ketosteroids (Androgen) in
urine samples. Practical Using venning methods.
2.8 Identify and determine pregnanediol in urine Identification of neutral 17.
(derived from progesterone) ketostroids (Androgens) in Using Kuber methods
2.9 Identify and determine estrogen in urine. urine samples.
2.10Determine adrenaline and non adrenaline by Practically identification and
ferricyanide method. determination of Pregnanediol
in urine (derived from
progesterone)
Practically identify and
determine the estrogen in urine.
Determine adrenaline and non
adrenaline by termcyanide
oxidation.
39
WEEK General Objectives : 3.0 Understand the mechanism of enzyme regulation/control.

3-4 Explain the need for the regulation of enzyme catalysed Demonstrations, classroom
biochemical reaction. discussions and lectures.
List types of enzymes regulation e.g.
(a) Allosteric
(b) Covalent modification
3.3 Describe the features of feed back control mechanism
in enzyme regulation.
3.4 Explain product inhibition in enzyme regulation.
3.5 Explain the term covalent modification. Lecture Teaching tools
40
WEEK General Objectives: 4.0 Understand the methods of PH fluid and electrolyte control in the body.
4.1 Explain, buffer systems. Teaching tools.
4.2 Explain the role of respiration in the control of
blood PH. Lectures and demonstrations, and
4.3 Explain the limitations of respiratory control of Assignments.
blood PH.
4.4 Explain major regulatory functions of the
kidneys.
4.5 Describe renal control of acid-base reabsorbed
secretion of Hx and synthesis of MHx salts.
4.6 Distinguish between respiratory and metabolic
acidosis.
4.7 Distinguish between respiratory and metabolic Lecture.
alkalosis.
41
WEEK General Objectives : 5.0 Understand the genetic factors that regulate the intracellular concentration of various proteins.
5.1 Explain the term gene. Discuss and Lecture the term gene. Teaching tools
5.2 Explain gene expression as form of protein synthesis Describe gene expression as form of
protein synthesis. “
5.3 Describe the general pathway for gene expression
(from gene to polypeptide products). “
Explain how regulation of gene expression may occur at Identify and lecture
one or several of the many steps in 5.3 above “
(transcription, modification, translation, etc).
Explain how operon is a coordinated unit on gene “
expression. “
Explain genetic elements of these operon are a regulator “
gene, as a operator gene and as a set of structural
gene, respectively. “
Describe hoe the regulator gene produces a repressor “
(protein) that can interfere with the operator gene.
Describe the effect of the binding of the repressor to the “
operator in the transcription of the structural gene. “
Describe the histidine operon as an example of “
repressible operon,
Describe two features of regulatory processes found in “ “
eukaryotic but not found in prokaryotic system
(hormone effects and protein stability). “
Describe the tryptophan pyrollax gene function to “
illustrate the two features in 5.10 above.
Explain how CAMP stimulate the transcription of several “ “
inducible operon.
“ “
42
NO PRACTICALS
WEK PRACTICALS TEACHERS ACTIVITIES RESOURCES

3-5 Isolate and purify hormones and hormonelike Practical isolation and Glass ware and reagent
substances from different laboratory animals and purification.
plants
43
PROGRAMME: BIOCHEMISTRY (HIGER NATIONAL DIPLOMA)
COURSE: NUTRITIONAL BIOCHEMISTRY I
CODE: STH 324
DURATION: 60Hours/15Weeks/ Lecture = 1 Tutorials = 0 Practical = 3
UNIT: 2.0
GOAL: This course is designed to provide the student with the knowledge of the
Biochemistry of food and nutrition in maintaining cellular function and integrity.
GENERAL OBJECTIVES: On completion of this course the diplomate should be able to:
1.0 Understand the role of carbohydrate, protein,and fat in the maintainance of integrity.
2.0 Understand the biochemical importance of vitamins and inorganic ions in nutrition.
44
Course: Nutritional Biochemistry II Course Code: STH 324 Contact Hours 60 Hours 1-0-3
Course Goal: The course is designed to provide the student with the knowledge of the biochemistry of food and the of nutrition in
maintaining cellular function and integrity.
WEEK General Objectives 1.0 Understand the role of carbohydrates, protein, and fat in the maintenance of the integrity
of the living cell.
Teaching Activities Resources
Demonstrations, exhibitions on Audio visual aids.
1-3 malnutrition.
4-7
NO PRACTICALS
45
PROGRAMME: BIOCHEMSITRY HIGER NATIONAL DIPLOMA
COURSE: PHYSICAL BIOCHEMISTRY II
CODE: STH 325
DURATION: 60Hours/14 Weeks (Lecture 2 Tutorials = 0 Practicals = 2
UNIT: 3.0
GOAL: This course is designed to provide the diplomate with a basic knowledge of physical biochemistry
GENERAL OBJECTIVES: On completion of this course, the diplomate should be able to:
1.0 Understand the application of thermodynamics and chemical equation
2.0 Understand the basic principles of enzyme catalysed reaction.
46
HND BIOCHEMISTRY
Physical Biochemistry II Course Code: STH 325 60 2-02
Course Specification:
WEEK 1.0 Understand the application of thermodynamics & chemical equilibrium
1-4 Special Learning Objective: Teaching Activities Resources
1.1 -Describe the three types of thermodynamic
systems as isolated, closed and open. Demonstrations Audio visuals
1.2 –Explain the thermodynamics of open systems. Classroom Models.
1.3 –Explain how a living cell constitutes an open Discussions and lectures
system. “
1.4 –Explain thermodynamic equilibrium. “
1.5 –Explain how chemical processes in the living “
cell are dynamic in nature. “ “
1.6 –State the 1st, 2nd and 3rd laws of
thermodynamics. “ “
1.7 –Explain the terms enthalpy entropy and free
energy. “
1.8 –Explain the relationship between enthalpy and “
free energy. “ “
47
WEEK 1.0 Understand the application of thermodynamics & chemical equilibrium
1-4 Special Learning Objective: Teaching Learning Activities Resources
1.9Explain the standard free energy of formation, and Lecture “
free energy change.
1.10 Explain the relationship between free energy “ “
change constant, PH and concentration.
1.10Explain the terms activity co-efficient and molar “ “
activity coefficient.
1.11Illustrate graphically the variation of Gibbs free “ “
energy (G) content with composition of reaction
mixture.
1.12Explain how enzyme catalysis does not alter “ “
chemical equilibrium but only quicken it’s
attainment by lowering the activation energy.
1.13 Distinguish between exorganic and endergomic “ “
reactions.
1.14Explain how reactions with + G” values are “ “
accomplished in the cell.
1.15Explain the term high energy compound. “ “
“ “
48
1.15Identify some high energy compounds that are used
as agent of coupling exorganic and endergonic “ “
reaction. “ “
1.16Describe the ATP cycle.
1.17Explain the standard free energy of hydralysis of “ “
ATP.
1.18Describe the structural basis of the free energy “ “
during hydralysis of ATP.
1.19Explain the transfer of phosphate Gps from ATP to
AMP and pyrophosphate.
1.20Describe the role of AMP and pyrophosphate.
49
WEEK General Objectives : 2.0 Understand the basic Principles of enzyme Catalysed reaction.
TeachersActivities Resources
Enzymes
Describe the distinctive features of enzymes e.g. Lecture Teaching tools
5-14 active site specifically etc.
Explain enzymes specifically as the basis of “
classification.
Determine acid and Alkaline phosphates optimum Carry out practicals on alkaline PH meter.
PH. phosphatase and PH – PH meter.
Determine the effect of activators and inhibitors Practical determination of effect
experimentally. of activators and inhibitors.
Explain and determine enzymatic catalysis Carry out experiment on the rate Practicals
measurement by the rate of disappearance of of enzyme catalysis. Practical
substrate or formation of products. - Enzymes different
Define enzyme activity and specific enzyme activity “ types
in international units (I>U) and S>I unit. - Reagents
Explain methods of enzyme assay. “
Carry out enzymatic assay of a coloured substrate
e.g. 4 nutropheny/phosphate by acid or alkaline
phosphate. - Burrettes
Describe the assay for enzyme activity for a turbid “ - Anvettes
substrate like milk e.g. xanthine oxidase in - Spectrophotometer
milk. “ - Chromatograph
Explain coupled enzyme assays. - “
50
WEEK General Objectives :
Illustrate 2.10 above with assay of the reaction F-G- “
P = G-G-P.
Explain how an enzyme reversibly combines, first with “
its substrate to form an enzyme substrate complex.
Explain why the process of product formation from 2.10
above is a slow process. “
Explain the term Rapid Equilibrium on the basis of 2.12
and 2.13 above. “
Explain steady state and Pre-steady state.
Illustrate 2.15 above with the equation. “
E +S ES “
OR
A B C
V1 V2 V3
Explain and determine enzyme-catalysed reactions
measurement under initial rate (Vo) conditions
Derive the Michealis-Menten equation from the Lecture and Carry out experiment to Practical
expression: measure velocity
k1 K3 “
E+S ES E+P
K2 k4
2.19 Explain the Kinetic constant, Km, Vmax, Kcat.
51
WEEK General Objective: Understand the basic Principles of enzyme Catalysed reactions.
Special Learning Objectives: Teachers/Learning Activities Resources

Explain the physiological significance of Km.
Describe the determination of Km and Vmax using line weaver Buck plots. Practical.
Show that Km and Vmax can also determined by Eddie-Hotset plots.
Carry out calculations/plots based on 2.17-2.20 above.
Determine experimentally, the Km and Vmax of an enzyme or fixed enzyme
concentration.
Define cofactors, activators, co-enzymes and prosthetic groups.
Explain how the rate of enzymatic catalysis can be affected by the presence of - Practical
cofactors and inhibitors. - Different enzymes
Define reversible inhibitors. - Spectrophotometer.
Distinguish 2.26 above using the line Weaver-Buck plots.
Distinguish between competitive, non uncompetitive inhibitors. “
Explain how some enzymes have more than one polypeptide chain. Teaching tools.
52
WEEK General Objectives: Understand the basic principles of enzyme catalysed reaction.
Special Learning Objective: Teachers/Learning Activities
Define allosteric enzymes.
Explain that allosteric enzymes are usually key “
enzymes in metabolic pathways. Carry out experiment on Electrophoretic tank.
Explain how allosteric enzymes obey sigmoidal electrophoresis using enzymes.
kinetics.
Describe the properties of allosteric enzymes. “
Illustrate 3.34 above with binding of oxygen to
heamoglobin.
Explain the hill equation.
Describe the properties and mode of action of “
aspartate isoenzymes. Teaching tools.
Explain isoenzymes. “
Distinguish isoenzymes from allosteric enzymes.
Illustrate experimentally the use of electrophoresis “
in the study of isoenzymes as being genetic
and post-translational. “
State the origin of isoenzymes as being genetic Laboratory practicals on liver Practicals
and post-translational. function and other organ Spectrophotometer
2.42Explain the importance of enzymes in functions. Blood samples.
developmental biology. “ - Practicals
- Same as above.
53
2.43Describe the uses of isoenzymes in biological Lecture

identification and classifications.
2.44Define Maker enzymes and enzymes “
compartilization.
2.45Describe the use of Maker enzymes in cell “
fractionation.
2.46List examples in 2.43 above. “
2.47Carry out the determination of GTP and ATP. Laboratory practicals on liver
2.48Carry out experimentally the marker enzymes for function and other organ functions.
liver function, postrate heart, kidney function etc.
using the serum.
PRACTICAL CONTENTS
WEEK PRACTICAL TEACHERS ACTIVITIES RESOURCES

5-14 Carry out enzymaticessay of goloared substrate Conduct practical on the rate of Reagents Different types of
e.g nutrophenylplosphate by acid or alkaline enzyme catalysis enzymes
phosphate Connect floste
2.40 Illustrate experimentally the use of Laboratory practicals on liver Blood samples
electrophocesis in the study of isoenymes as function and other organ spectrophotometer
being genetic and post translational functions
2.48 Carry out experimentally the nmarker
enzymes for liver function, postrate, heart, kidney
functions etc using the serum
54
COURSE: BIOCHEMICAL METHOD II
CODE: STH 321
DURATION: 75Hours/15Weeks (2Hours Lecture, Tutorials 0 3 hours practical
UNIT: 3.0
GOAL: This course is designed to enable the diplomate with a clear understandingof the
Principle and application of biochemical methods.
GENERAL OBJECTIVES: On completion of this course the student should be able to:
1.0 Understand electrophoresis as a method of separation and identification based
on movement of charged molecule.
2.0 Understand the principle application of spectrophotometrey
3.0 Understand the principle and application of spectro flourimetry.
4.0 Understand the principle and application of chromatography methods.
5.0 Understand the principle and application of the potentiometric methods.
55
Course: BIOCHEMICAL METHOD. II Course Code: STH 321 Contact Hours 75 Hours 2-0-3
GOAL: This course is designed to enable the student with a dear understanding of the principle and application of biochemical
methods.
WEEK General Objectives : 1.0 Understand electrophoresis as a method of separation and identification based on
movement of charged molecules.
Special Learning Objective: Teaching Learning Activities Resources
1-2 1.0 Understand electrophoresis as a method of Carry out experiment on

separation and identification based on movement of separation techniques using
charged molecules in an electric field. electrophoretic apparatus.
Electrophoresis
1.1 Define electrophoresis.
1.2 Explain the principles/theory of electrophoresis.
1.3 Explain the factors that govern the behaviour of
charged particles in an electric field. Practical
1.4 Describe the effect of the mobility particles (e.g
PH osmotic flow, diffusion, etc.) during
electrophoresis. “
1.5 Describe the effect of the intensity of an electric
field, power supply, current type of buffer used
etc. on electrophoretic run.
56

1.6 Demonstrate electrophoretic run in gel. Drawing studio.
1.7 Draw the circuit diagram of an electrophoresis power Practical demonstration in lab.
supply. Conduct studio drawing.
1.8 Describe the precautionary measures adopted in high
voltage Electro-phoresis. Electrophoretic material.
1.9 Describe and apply methods of sample application
and markers/standards in Electrophoresis. Conduct practical.
1.10Detect and estimate sample components. “
1.11Identify in electrophoresis the different types of “
support media. Conduct practical.
1.12Prepare different support media. Demonstrate experiment on sample
1.13Describe the different types of electrophoresis e.g separation.. “
high voltage, moving boundary, Iso-electro focusing
etc. Demonstrate the different types of
1.14List the application of electrophoresic. electrophoresis.
1.15Identify voltage, movement of ion (in cm) and
Development time in Electrophoretic run repor
WEEK General Objectives : 2.0 Understand the Principle of Spectrophotometry
57
Spectrophotometry
2.1- Explain the electromagnetic emission spectrum. Demonstrate the spectrum.

3-4 2.2- Explain the theory of light absorbtion and
transmission (Beer lamber law).
2.3- Draw a schematic digram fo U.V/visible Studio drawing.
spectrophotometer (poer supply, sight sources,
manochromators, detecto and measuring device).
2.4- Identify the five main sections of spectrophotometer Makes sketches for grading.
(radiation source, monochromator, photometer, sample
area and detector area).
2.5- Describe the types of light sources, cells regions of
the spectrum covered by visible and U.V
spectrophotometer.
2.6- Describe the operation of the spectrophoto meter. Supervise students use the Spectrophotometer.
2.7- Describe the transmissive power of solvents (against spectrophotometer.
distilled water).
2.8- Describe the absorbance characteristics of some Demonstrations using Teaching tools.
compound, e.g potassium dichromate, Haemoglobin etc. spectrophotometer.
2.9- Describe ultraviolet spectrum as plot of the wave “
length or frequency of absorption versus the absorption
intensity.

58
Explain the Expression = A “ Teaching tools
60
For intensity absorption. “
Explain the effect of PH on absorption spectra. “
Explain the term ‘Chromaphoresic’ anxochrome batha
‘chromic shift’ hyperchronic effect.
Describe and apply the precautions for effective sample Laboratory demonstration. Spectrophotometer
handling in spectrophotometry.
List applications of u.v./visible spectrophotometers.
Determine and maintain a catalogue of the spectra for Practicals using spectrophotometer.
important biological compounds. Grade results.
Identify components for a mixture (e.g drug) from their “
absorption spectra.
Produce standard curves and determin the concentration Experiment on absorption spectral
of sample solution from these curves. method.
Explain enzyme activity by u.v. spectraidin absorption. Practicals using spectrophotometer.
Explain enzyme activity by u.v spectraidin absorption.
59
Spectroflourimetry
5-6 Explain the phenomenon of fluorescence. Demonstration and lectures.
Explain that the intensity of fluorescence is properties to “
the concentration of the substance in solution.
Explain the Phenomenon of “quenching”.
Identify the parts of a spectroflourimeter light sources, “
monochromator, light trap, photomultoplic recorder. Grade sketches. Spectroflourimeter.
Describe diagramatically, the outlay of a
spectroflourimeter.
Describe the methods of preparation of a sample for “
analysis by spectroflourimetry.
Prepare sample for analysis by spectroflourimeter.
Describe the operations of a flourometer.
Explain the applications of flourimetry and its limitations Practical sample preparation. “
in analytical work.
Prepare standard curves for spectroflourimetric
determination.
Analyse samples using spectroflourimeter.
Practical sample analysis. “
60
Chromatography
Explain the term chromatography. Demonstration and lectures. Various
7-9 Describe the various principle of chromatography. chromatrographic
Classify types of chromatography: Supervise student’s practicals. equipment and
Liquid-solid, liquid-liquid, and gas-liquid instruments.
Carry out thin layer and paper chromatograph. Chromatography
Explain the following terms used in chromatography:- RF “ apparatus.
values, solvent front, pertition coefficient,stationary
and mobile phases, retention time.
Identify types of absorbents and ion-Exchange resins
used in chromatography. Practical identification and Absorbents.
Describe the chromatography properties of absorbents discription of absorbents and ion
and ion-Exchange resins. E.g. absorbtive powers, exchange resins.
weak and strong Exchangers etc. “
Desribe different methods of developing chromatograms
e.g sample elution, frontal analysis and gradient
elution.
Identify solvents used in chromatography and describe
their eluting powers and properties. Practical identification.
Describe the process of thin layer chromatography
(TLC). Demonstrate the process.
Carry out separation using thin layer chromatography.
Grade practicals. TLC materials
61
Special Learning Objective: Resources

Describe methods of spreading layers in T.L.C.
9-10 Describe methods of preparation, application and Demonstration
location of samples in TLC. Demonstration TLC samples
List and identify locating agents.
Described methods of identification of components of Practical identification. Locating agents.
TLC. “
Carry separations using thin layer chromatograph. TLC materials.
Explain the principle of gel-permeation (molecular Conduct and grade practicals.
steve) chromatography.
62
Gel permeation chromatography
Identify the media used for gel-permeation Practical identification.
chromatography (e.g gel-resins).
Describe gel-permeation chromatography.
Find the molecular weight of macromolecules (e.g Conduct and grade practical on use Permeation
proteins) using permeation chromatography. of permeation chromatography. chromatography.
Describe the relative advantage/disadvantages of the
various media used in permeation chromatography
above.
Biological affinity chromatography
Explain the bases for biological, affinity chromatography.
Describe biological affinity chromatography.
Identify the matrices for gel-affinity chromatography.
Explain the characteristics of the matrices for gel
permeation chromatography. Demonstration and lectures. Biological affinity
4.26Describe the procedure for the linkage of ligand and Practical identification. Chromatography.
supporting matrix (Activiation of matrix and
coupling to ligand)
63
Gas-liquid chromatograph
Describe gas-liquid chromatography as a form of column
10 -12 chromatography in which the stationary phase is
liquid and the mobile phase is a gas.
Illustrate diagrammatically the arrangement or layout of Drawing. Gas-liquid-
the components of a gas-liquid, liquid-liquid chromatograph
chromatography.
Identify different types of detectors e.g thermal Practical identification of detectors Various detectors.
conductivity detector, flame cornization detector,
electron capture detector.
Separate samples using GLC. Practical separation and reports. Gas-liquid
Explain the working of various detectors in 3.26 above. chromatograph.
Special Learning Objective: Resources

Column chromatograph
Describe the various methods of column preparation i.e. Supervise column preparation. GLC, liquid-liquid
packing of column (e.g. Dry and wet packaging). chromatograph.
Prepare columns.
State the relative advantage of the different methods of
column preparation in 4.31 above.
Describe the preparation and application os samples for Practical preparation of samples and
gas-liquid/-liquid chromatography. application.
Prepare and apply samples in gas-liquid, liquid-liquid
chromatograph.
Determine column efficiency, adjusted retention time.
Determine kovat indeces and MCR cynold constants
64

Compare the values in 3.32 above with those in the
relevant literature.
List the applications of the various chromatographic
techniques.
Absorition chromatography
Carry out absorption chromatography. Conduct practical and grade results. Absorption
Prepare column and sample for chromatographic “ chromatograph
separations. “
Recondition absorbents. “
Determine the choice of absorbents for a “
chromatographic separate.
Measure R.F values. “
65
WEEK General Objectives : 5.0 Understand the Principle and application of potentiometric methods.
Potentiometric methods
13-14 Explain the relationship between the electrode potential Demonstration and lectures.
of a reference electrode and the ionic concentration Teaching tools.
of the solution in which it is immersed:- i.e
E = E - RT in C (nerst Equation)
Ref F
Explain the relationship between electrode potential and
PH i.e “
E = E + 2.303RT (PH outside) “
F
Describe a PH meter as a precision instrument for PH
measurement. Demonstration.
Identify the components of a PH meter. PH meter.
Describe the functions of the components of 7 PH Practical identification and sketches.
meter. “ “
66
Draw the diagram of a PH meter. Grade drawings.
Explain with examples, the term “ion-specific
electrodes”.
Describe the set-up for a potentiametric titration with the Grade diagram
aid of a schematic diagram.
List and explain the application of potentiometric “ PH meter
measurements in biochemical analysis. “
Calibrate the PH meter. Practicals “
Measure the PH of a solution using PH meter. “
Determine the pcb and pka values from titration, data. “
Compare Experimental results with calculated results
from :
PH = pka + log (salt)
(Base) Electrode.
Calibrate the electrode.
Describe and apply the use of calibrated electrodes in Practical calibration, Grade results.
respiratory and photosynthesis (gas exchange). Practicals.
67
WEEK PRACTICALS TEACHTERS ACTIVITIES RESOURCES
1-2 1.0 Cary out method of separation and Conduct practical on Electrophoresis tank
identify feat ion based on the movement of separation techniques using
charged molecules in an deictic field. electrophoresis apparatus
3.7 Prepare sample for analysis by Practicals on sample Spectroflorimeter

spectroflourimeter. preparation
3.10Prepare standard curves for
5-6 spectroflorimeter Practicals on standard curve Spectroflorimeter
preparation
Supervise student’s practical
Cary out thin layer and paper on thin layer and paper
chromatography graph. chromatography
4.10Carry out separation using thin layer Conduct practical on
7-9 chromatography. separation techniques using
(TIC)
4.29 Separate samples using GLC Practical separation and Gas liquid chromatography
reports
4.32 Prepare columns Gas liquid chromatography
4.35 Prepare and apply samples in gas-liquid Supervise column preparation
chromatography Practical preparation of
samples and application
4.39 Carry out absorption chromatography
Conduct practical on
absorption chromatography Absorption chromatography
4.40 Prepare column and sample for and grade result
chromatographic separation Supervise column preparation
and sample separation
5.10 Calibrate pH meter Supervise students to calibrate pH meter
13-14 pH meter
5.11 Measure the pH of a solution using pH Conduct practical on pH meter pH meter
meter
5.14 Calibrate electrode Supervise students to calibrate Electrode equipments
electrode
68
PROGRAMME:HND BIOCHEMISTRY
Course: INTERMIDIARY METABOLISM I Course Code: STH 322 Contact Hours75 hours 2-0-3
GOAL: This course is designed to acquaint the student with the principles involved in intermediary metabolism
WEEK General Objectives: 1.0 Understand the Phenomenon of intermediary metabolism
1-3
Intermediary metabolism
1.1 Explain that metabolism in a living cell Illustrated lectures. Charts and audio visuals.
constitute catabolic (breakdown) and anabolic
(synthesis) processes which occur
simultaneously. “
1.2 Explain intermediary metabolism as the “
interchangeability of derivatives (metabolites) of
carbohydrates, proteins and fats (lipids) via
reactions mediated by appropriate enzymes and
coupled by relevant coenzymes/cofactors.
1.3 Illustrate and explain intermediary metabolism “
by a simple schematic diagram e.g.
1.4 Illustrate the central role of acetyl Coa
intermediary metabolism.
1.5 Describe how the energy for cellular metabolism
is derived from the break down of acetyl COA. “
1.6 Explain how the energy from 1.5 above is
captured ina the form of ATP (adenosine “
triphosphate) which is revisable.
“
69
WEEK General Objectives:

1.7 Describe ATP as the universal energy currency in “
biological systems.
1.8 Explain how energy released from the degradation of “
some substrates may be utilized in the formation of
other cellular components.
1.9 Explain that the sum total of breakdown of “
carbohydrates, fats and proteins is a chain reaction
involving transfer of reactions which lead to the final
products of cellular respiration (Co2 + H2o) and
ATP.
1.10Describe the ATP cycle and explain how ATP forms “
the energy currency in biological system.
70
WEEK General Objectives: 2.0 Understand the Pathways of carbohydrate, protein and lipid metabolism.
4-6 Nutrient metabolism
List the enzymes and products of digestion of Illustrate lectures
carbohydrate.
Explain the term substrate level phosphorylation. “
Define glycolysis as the pathway of breakdown of “
phosphorylated sugars to provide and lactate.
Describe the glycolytic pathway and the conversion
of pyruvate to acetyl COA. “
List the key enzymes of glycolysis.
Identify the steps that consume or yield energy in “
glycolytic pathway. “
Deduce the net energy yield of this glycolytic
pathway. “
Distinguish between aerobi and anaerobi glycolysis.
Describe the alternative pathway of glucose oxidation “
(pentose phosphate pathway/hexose
monophosphate shunt) “
State the biochemical importance of 2.9 above.
Describe glucogenesis, gluconeogenesis, slycogeresis
and glycogenelysis. “
Describe cori cycle.
71
WEEK General Objectives : 2.0 Carbohydrate Metabolisim
Special Learning Objective: TeachersActivities

2.13 Explain Pasteur effect. “
2.14Define oxidation of fatty acids. “
2.15Describe the processes occurring in fatty acid “
oxidation (activation dehydrogenation, hydration,
further dehydrogenation and Thiaclastic cleavage).
2.16 Explain how all reaction of B-oxidation of fatty acid Lecture
are reversible.
2.17 Explain how fatty acids undergo activation in the “
cytosol and enters the mitochondrior where it
undergoes B-oxidation.
2.18Describe the B-oxidation of fatty acids to acetyl “
COA. “
72
2.19 Explain that the acetyl COA produced in fatty acid
oxidation enters the TCA cycle for further
degradation.
7-8 2.20 Describe the oxidation Via propionic acid of Practical on unsaturation.
branched and odd-numbered fatty acids.
2.21Determine degree of unsaturation and unsaponifiable “
fraction.
2.22 Explain that FADH2 and NADH + H+ produced in
fatty acid oxidation are also oxidized through the
electron transport system of the mitochondria “
eventually by molecular oxygen.
2.23 Determine the energy yield in terms of ATP
molecules for the complete degradation of a named “
fatty acid e.g. palmitic acid or oleic acid.
2.24 Compare the energy yield when one mole each of
saturated and unsaturated fatty acid of equal chain
length is completely oxidized.
2.25Describe the formation and metabolism of ketone
bodies (acetone, acetoacetate and P-hydroxy butyrate).
Describe the biosynthesis of fatty acids.
Describe the two pathways of fatty acid biosynthesis
(cytoplasmic mitochondrial).
Explain that the cytoplasmic pathway is the major
pathway of fatty acid synthesis.
Describe the biosynthesis of triglycerides and
phosphatides (phospholipids).
Describe the biosynthesis of sterols from cholestrol.
Identify experimentally metone bodies in abnormal
urine.
List the enzymes and products of protein digestion.
Explain how amino acids can be a source of cellular
energy (surplus amino acids).
73

2.26Explain how acetyl COA also acts as precursor in the Practical determination of ketone
9.10 biosynthesis of fatty acids. bodies and chlestraol level
2.27 Carry out determination of ketene bodies,
cholesterol level.
2.28 Describe the biosynthesis of fatty acids.
2.29 Describe the two pathways of fatty acid biosynthesis Illustrate lectures.
(cytoplasmic mitochondrial).
2.30 Explain that the cytoplasmic pathway is the major “
pathway of fatty acid synthesis.
2.31 Describe the biosynthesis of triglycerides and
phosphatides (phospholipids). Practical identification of ketone
Describe the biosynthesis of sterols from cholestrol. bodies in urine.
Identify experimentally ketone bodies in abnormal urine.
List the enzymes and products of protein digestion.
Explain how amino acids can be a source of cellular
energy (surplus amino acids).
74
Explain how the c.Skeleton of amino acids are either
converted into fatty acids are either converted into
fatty acids and glucose or oxidized via the TCA
cycle.
Explain the terms, ketogenic and glucogenic amino Conduct practicals on tests for urea.
acids.
List ketogenic and glucogenic amono acids.
Explain transmination and oxidative deamination.
Write chemical equations to illustrate the process in 2.37
above.
Describe the formation of urea (urea cycle).
Test for urea in urine qualitatively and quantitatively.
75
WEEK General Objectives :3.0 Correlations in Intermediary metabolism
Special Learning Objective: Teachers Activities

Explain that for each molecule of NADH + H + oxidized, “
3 ATP molecules are produced and for each molecule
11 - 12 of FADH2 oxidised 2 molecules of ATP are formed.
Determine the number of molecules of ATP produced per
molecule of pyruvate. Calculations.
Determine the number of molecules of ATP produced by
the complete degradation of a molecule of glucose. “
Determine the number of ATP molecules produced in
eukayotes and prokaryotes from the complete
degradation of 1 molecules of glucose. “
Explain the TCA cycles as th common pathway for the
degradation of products derived from carbohydrates,
lipid and protein metabolisms and synthesis of other “
substrates and compound (e.g haem-nny system and
amino acid) via ketoglutarate carbohydrates via
oxalacetate and phosphen al pyruvate or c-skeleton of
fats.
State that nearly all the Co2 is produced in the TCA cycle.
76
Special Learning Objective: TeachersActivities Resources

13-14 Explain that most of the energy from the decomposition “
of food stuffs is produced in the respiratory chain.
Explain that in micro-organism a variation of the TCA
cycle (viz the glycoxylate cycle) is obtained. “
Explain why in the glycoxylate cycle the emphasis is not
on degradation of acetate but rather on synthesis of “
succinate, malete and oxaloacotate (and eventually of
carbohydrates) from acetyl COA.
Illustrate with the aid of a schematic diagram, the
glyoxylate cycle. “
Explain why the glyoxylate cycle does not exist in the
mammaliam organisim. “
Eplain how the glyoxylate cycle plain a domanant role in
plant seedings, which utilize fat reserves for synthetic “
purposes, and in microorganisms which grow on
fatty acids or acetic acid as an exclusive carbon
source.
State the features of the ETC.
Explain the effect of inhibitors on the respirators chain. Lecture.
Explain that the ETC takes place in the membranes.
Identify the different levels of cellular regulations of
metabolic pathways. “
“
77
WEEK PRACTICALS TEACHERS ACTIVITIES RESOURCES
9-10 2.33 Test for ketone bodies in abnormal urine Practical identification of Sample of urine
ketone bodies in urine
2.42 Test for urea in urine quantitatively and Test for urine Sample of urine
qualitatively
78
COURSE: INTERMIDIARY METABOLISM II
CODE: STH 411
DURATION: 60Hours/14 Weeks / Lectures = 1 Tutorials = 0 Practicals = 3
UNITS 2 Units
GOAL: This course is designed to enable the diplomate with the principles involved in
Intermediary metabolism
GENERAL OBJECTIVES: On completion of this course, the diplomates should be able to:
1.0 Know the common pool of intermidiary
2.0 Understand nucleic acid metabolism and protein biosynthesis
3.0 Understand nucleic acid metabolism and protein biosynthesis
79
Course: Intermediary Metabolism II Course Code: STH 411 Contact Hours 60 Hours 1-0-3
Course Goal: The course is designed to acquaint the students with the principles involved in intermediary metabolism.
80
WEEK General Objectives: 1.0 Know the Common\pool of Intermediary Metabolism
1.1 escribe the metabolic chart (a comprehensive
1-3 diagrammatic sketch of the metabolic pathways.
1.2 Explain that metabolic chart reveals that various Illustrated lecture
food shifts and endogenous substances are
broken down constantly to produce common “
intermediates (common pool of metabolites) e.g.
acetyl COA, Pyruvate and ketoghitarate,
succinate, oxaloacetate, H2, ATP etc.
1.3 Explain that theoretically a specific metabolic
pool exists for every substrate.
1.4 List the numerous inlets and outlets of metabolic “
pool.
1.5 Describe the outlets flows to the TCA cycle to “
fat synthesis, and to isoprenoid synthesis.
1.6 Describe how molecules are mixed uniformly in “
such a pool.
1.7 Explain that once submerged in the metabolic “
pool the origin of a given, molecule (e.g. acetyl
CoA), whether from fat, carbohydrate or surplus “
amino-acid, can no longer be started with
certainty.
1.8 Explain how the spread of radioactively labeled
fragments over the entire organisms is as a result
of 4.7 above. “
81
WEEK General Objectives: 2.0 Understand nucleic acid metabolism and protein biosynthesis.
4-6 Special Learning Objective: Teachers Activities

.
2.1 Describe the degradation of purine in man and other Lecture
primate to produce uric acid.
2.2 Describe the break down of uric acid by some “
mammals to allantoin.
2.3 Describe the degradation of pyrimidine. “
2.4 Describe the methods of excretion of pyrimidine “
nitrogen.
2.5 Explain how pryrimidine breakdown may occur “
while the pyrimidine base is still attached as the
nucleotide or nuclea side.
2.6 Describe and identify the causes and symptoms of “
the disease gout in in man.
2.7 Describe the reactions involved in the biosynthesis of “
purine nucleotides.
2.8 Describe how the various components of the purine “
ring are derived from formate, Co2, glutamine,
aspertate and glycine.
2.9 Compare the pathways of purine synthesis in micro- “
organisms with those found in the liver of animals.
2.10Explain why pureness are synthesized de novo, not as
free purines, but first as the nucleotide inosinic acid
which is then converted into adenine and guanine
nuclectides.
2.11List the enzymes and co-factors in the reaction in
2.10 above.
82
WEEK General Objectives : 2.0 Understand Nucleic acid
metabolism and protein biosythesis.
7-9 Special Learning Objective: Teachers/Learning Activities Resources
2.12 Describe the reactions involved in biosynthesis of “
the pyrimidine ring.
2.13 Describe the subsequent synthesis of pyrimidine “
nucleotide starting with orotic acid as precursor.
2.14 List the enzymes and co-factors on the reaction on “
2.10. above.
2.15 Explain the role of NDA on a carrier of genetic “
information.
2.16 Describe the biosynthesis of DNA and RNA. “
2.17 Explain the Watson-crick model of the DNA and it “
is replication .
2.18Describe the semi conservative replication of DNA. “
2.19 Describe the Meseion –state experiment for the “
demonstration of semi-conservative replication of
DNA.
2.20 Describe the 3 main steps involved in replication of Lecture
DNA (initation, elongation and termination).
2.21 Explain the role of enzymes polymerase and “
unwinding protein in DNA replication.
2.22 Describe the process by which the cell regulated its “
DNA synthesis.
2.23Describe the process by which the cell regulated its
DNA, resulting from physical, chemical or “
environmental processes.
2.24 Explain mutagenesis.
83
WEEK General Objectives: 3.0 Understand nucleic acid metabolism and protein biosynthesis.
10 - 12 Special Learning Objective: Teachers/Learning Activities

Nucleic acid metabolism and protein synthesis
3.1 explain how and why amino acids are activated as a Lecture
pre-requisite in protein synthesis.
3.2 Explain how activated amino acids are linked to “
transfer RNA (+RNA) by specific synthesis
(aminoacyl) +RNA synthesis)
3.3 Explain how the fidelity of protein synthesis depends “
on the high specificity of aminoacyl + RNA
synthetase.
3.4 Describe the nature of the + RNA. “
3.5 Explain the suppression of other mutation by mutant “
+ RNA.
3.6 Describe the process of protein synthesis in the rough “
endoplasmic reticulum in ribosomes.
3.7 Describe the structure of the ribosomes – the “
organelles of protein synthesis.
3.8 Explain that at RNA molecule may recognize more “
than one cadon because of wabble.
3.9 Explain how proteins are synthesized in the amino-to “
carbexy direction.
3.10Explain that messenger RNA (m RNA) is the carrier “
of the specific genetic information on protein to be
synthesiszed
84
WEEK General Objectives : 3.0 Understand nucleic acid metabolism and protein biosynthesis

3.11explain that messenger RNA is translated in the 5”- Lecture
3” direction.
3.12 Explain how several aribosornes simultaneously “
translate a mRNA molecule.
3.13 Explain the initiation of protein synthesis “
formylmethianine +RNA.
3.14 Explain the process by which an elongation factor “
delivers aminoacyl +RNA to the appropriate site on
the ribosome.
3.15 Explain the formation of peptide bond followed by “
translocation.
3.16Explain the process of termination of protein Carry out experiment on blood
synthesis by release factors. sample’s separation.
3.17 Explain the process of protein modification
following translocation. Practical isolation and separation
3.18 Separate serum protein. of nucleic acid.
3.19 Determin protein content of liver homogenate or Practical measurement of nucleic
serum by Biuret or lowry methods. acids.
3.20 Isolate and separate nucleic acids. Practical determination of bare
3.21 Measure and identify nucleic acids. composition of nucleic acids.
3.22 Determine base composition of nucleic acids.
85
13-14 3.18 Separate serum protein Carry out experiment on blood Blood samples
separation
3.20 Isolate and separate nucleic acid Practical isolation and

separation of nucleic acid
3.21 Measure and identify nucleic acid Practical measurement of

nucleic acid
86
PROGRAMME: BIOCHEMISTRY HIGER NATIONAL DIPLOMA
COURSE: NUTRITIONAL BIOCHEMISTRY II
CODE: STH 412
DURATION: 60 Hours/15 Weeks/Lecture =2 Tutorials=0 practicals=3
UNIT: 2.0
GOAL: This course is designed to provide the diplomate with the knowledge of the biochemistry
of food and the role of nutrition in maintaining cellular functions and integrity.
GENERAL OBJECTIVES: On completion of this course, diplomate should be able to:
1.0 Understand principles and practice of nutrition
2.0 Understand food spoilage and the nutritional importance of food processing
and preservation.
87
Course: Nutritional Biochemistry II Course Code: STH 412 Contact Hours : 60 Hours 1:0:3
Course Goal: This course is designed to provide the student with the knowledge of the biochemistry of food and the role of nutrition
in maintaining celluar functions and integrity.
WEEK General Objectives : 1.0 Understand the Principles and Practice of Nutrition

1-4 1.1 Explain general nutritional requirements and Illustrated lectures. Nutritional charts
energy aspects of diets in man.
1.2 Explain basal metabolic rate (MBR). “ Audio visuals.
1.3 Describe the major nutritional disorders in man “
e.g obesity, kwashiorkor, merasmus.
1.4 Describe methods involved in nutrition research. “ “
1.5 Explain the effects of diet in physiological “ “
processes in man.
1.6 List primary nutritional disorders (e.g. deficiency “ “
diseases).
1.7 Explain conditional nutritional disorders. “ “
1.8 Describe the relationships between nutrition and “ “
public health (effects of carcinogens, enzyme
inhibitors and microbial contamination).
1.9 Explain the roles of diets (low-protein, protein- “ “
free, vitamin-free, high fat etc) on metabolism of
drugs and other foreign chemicals in man.
1.10Proximate analyses of food, including beverages. Conduct practicals on Chromatographic equipment
1.11Determine experimentally Biololgical values proximate analysis in 1.10 and Spectrophotometer khjadal
(BV) of food. 1.11. apparatus soshlexapparatus
1.12Determine experimentally, Net protein utilization Practical determination Glasswares.
(NPU) on NPU. Food items.
88
1.13Estimate Vitamins and mineral contents of food. Practical identification, “

1.14Identify toxins in foods. Vitamins, minerals and toxins “
89
WEEK General Objectives : 2.0 Understand food spoilage and the nutritional importance of food processing and preservation
5 - 14 2.1 Explain food spoilage. Demonstration Samples of spoiled food

2.2 Explain the cames of food spoilage. Lecture items.
2.3 List different types of food spoilage. “
2.4 Outline various techniques of food processing and “
preservation. “
2.5 Explain how food processing enhances digestibility
and palatability. “
2.6 Explain how processing of food can detoxify food
(e.g. cassava cyanide) or produce toxins
(Nitrogamines) “
2.7 Explain how food processing can destroy Food samples.
endogenous enzyme inhibitors, vitamins etc. Lecture
2.8 Explain food processing as a means of preservation.
2.9 Explain the importance and harzards of food “
additives. “
2.10Explain how some food processing techniques (e.g
cooking) can adversely affect vitamin availability. “
2.11Explain how storage of fats and oils can make them
go rancid due to oxidation. “ Samples of rancid oil
2.12Explain why a rancid fat (oil) has a high content of
free fatty Acid (FFA) . “
2.13List unconventional sources of food protein eg leaf Food samples
protein (cassava) fermentation of waste single cell “
protein.
90

2.11Explain how storage of fats and oils can make them Lecture
go rancid due to oxidation.
2.12Explain why a rancid fat (oil) has a high content of “
free fatty Acid (FFA).
2.13List unconventional sources of food protein eg leaf “ Food samples
protein (cassava) fermentation of waste single cell protein
(SCP). “
2.14Formulate and develop nutritive foods. “ “
2.15Explain food texture and nutritive value. “ “
2.16Explain quality control in food “ “
manufacture/formulation/development.
2.17Explain food fortification eg with mineral and “ “
vitamins..
2.18Explain food supplementation. “ “

1-4 1.11 Determine experimentally biological Conduct practical on proximate Khjadal apparatus
value (BV) of food. analysis Soxhlet apparatus
1.12 Determine experimentally net protein Practical determination of NPU
ultilization (NPU) on NPU. ultilization
Glass ware
1.13 Carry out practical on vitamins and Practical identification of Food items
mineral contents of food vitamin and minerals
91
PROGRAMME: BIOCHEMISTRY HIGER NATIONAL DIPLOMA
COURSE: BIOTECHNOLOGY AND GENETIC ENGINEERING
CODE: STH 413
DURATION: 60Hours/15Weeks/ Lecture=1 Tutorial=0 Practicals=3
UNIT: 3.0
GOAL: This course is designed to enable the diplomates to understand the manupulaion
of the genetic coding of micro organisims for the benefit of technology.
GENERAL OBJECTIVES: On completion on this course, the diplomate should be able to:
1.0 Understand the concept of biotechnology and genetics engineering.
2.0 Understand the significance of biotechnology to medicine
3.0 Understand biotechnology processes.
4.0 Understand the technology of plant and animal cell culture.
5.0 Understand genetics and biotechnology.
6.0 Understanding the concept of genetic engineering.
7.0 Understanding the concept of single cell protein production.
8.0 Understanding the use of isolated biological units or enzymes in industry
and medicine.
9.0 Understanding biological fuel generation in biotechnology.
10.0 Known the application of biotechnology in agriculture and forestry.
11.1 Understand the role of biotechnology in environment technologic.
92
Course: Biotechnology and Genetic Engineering Course Code: STH 414 Contact Hours : 30 Hours
Course Goal: Understand the manipulation of the genetic coding of micro-organisms for the benefit of technology
WEEK General Objectives : 1.0 Understanding the Concept of Biotechnology and Genetic Engineering.
Special Learning Objective: TeachingActivities Resources

1-2 1.1 Explain the terms Biotechnology and genetic Illustrated Charts
engineering. Lectures Audio visuals
1.2 List the various disciplines that constitute “
Biotechnology.
WEEK General Objectives : 2.0 Understand the significance of Biotechnology to medicine.
2.1 Explain the term antibiotics. Lecture. Charts

2.2 Describe the roles of biotechnology in the production “ Audio visuals
of antibiotics.
2.3 Describe the roles of biotechnology in the production “
of Hormones. “
2.4 Describe the biotechnology of vaccines and “
monoclonal antibodies productions.
93
WEEK General Objectives : 3.0 Understand Biotechnological processes.
3-4 3.1 Explain fermentation technology. Lecture. Laboratory fermentor

3.2 Explain the roles of Biochemists, Microbiologist and “ “
chemical engineers in the development of
fermentation processes.
3.3 Described openand closed fermenters systems. “ “
3.4 Describe the stages of fermentation process. “ “
WEEK General Objectives : 4.0 Understand the technology of Plant and animal cell culture.
4.1 Explain cell culture. Illustrated lectures. Media

4.2 Describe methods of mass cultivation of organisms “ “
for biotechnological processes e.g bacteria, yeast,
filamentous fungi, plant cell cultures.
94
WEEK General Objectives : 5.0 Understand genetics and biotechnology.
5.1 Identify microorganisms used in biotechnological Microbiological identification Microscopes,

5-6 processes. and drawings. Culture media.
5.2 State the properties of microorganisms in 5.1 above. “ “
5.3 Distinguish between structure and regulatory genes. Illustrated lectures Charts and audio visuals.
5.4 Describe the steps involved in the modification of “ “
genes to improve productivity e.g. in Enzymes
production, bye-product formation improvily yields
of metabolites etc. “
5.5 Describe the techniques for 5.4 above e.g screening, “
selection etc. “
5.6 Explain the roles of mutation and recombination in “
modification of organisms genome. “
5.7 Describe the processes that facilitate the transfer of “
genetic materials from one organism to another e.g
transformation, transduction etc. “
5.8 Explain protoplasm fusion and DNA compatibility. “ “
5.9 Explain the application of protoplast fusion in yield “
improvements e.g facilitating recombinant DNA
transfer, improvement of antibiotics etc.
95
WEEK General Objectives : 6.0 Understand the Concept of Genetic Engineering.
6.1 Explain the term Genetic Engineering or cloning. Illustrated lectures Audio visuals
6.2 Describe the process of gene transfer technology i.e. “ “
vector or carrier system e.g. splicing system,
introduction of vector DNA recombinants.
6.3 List the bioharzards associated with genetic Lecture. Teaching tools
engineering.
WEEK General Objectives : 7.0 Understand the Concept of Single cell protein production.
7-8 7.1 Explain the term single cell protein (SCP) and the Illustrated lectures Audio visuals
need for protein.
7.2 List the sources and how SCP is derived from high
energy source e.g methanal, gas oil attenoy etc.
7.3 Describe the processes involved in the utilization of “ “
waste for the production of SCP.
7.4 Explain the advantages of using organic wastes for Lecture “
SCP production.
7.5 Describe the processes involved in the utilization of “ “
complex lingo-cellulose wastes for SCP production.
7.6 Describe the use of agricultural crops, algae etc. in “ “
the production of SCP.
7.7 Explain the economic implication of SCP. “ “
96
WEEK General Objectives : 8.0 Understand the use of isolated biological units or enzymes in industry and medicine.

8.1 Explain the term enzyme technology or engineering. Illustrated lectures Audio visuals, charts.
9 - 10 8.2 Identify the various areas of enzyme technology e.g. “ “
in production, isolation, purification, immobilization
etc. “
8.3 Explain the importance of enzyme technology in “
solving problems in food production, energy
shortage, food preservation and improvement of the
environment.
8.4 Explain the various areas of industrial application of “ “
enzymes e.g. in biological detergents baking
industry, dairy industry, starch industry, textile
industry, leather industry, medical and
pharmaceutical “
8.5 Describe the methods of enzyme production. “ “
8.6 Explain immobilization of enzymes on insoluble “
polymers e.g. membranes, particles etc. “
8.7 Explain the various areas of application of “
immobilized enzymes in industrial processes e.g.
production of organic acids, fructose syrup etc.
8.8 List the advantages of using immobilized enzymes or “
biocatalyst in industrial processes.
8.9 Describe the methods of enzyme immobilization. “
Physical and chemical methods.
97
WEEK General Objectives : 9.0 Understand biological fuel generation in biotechnology.
9.1 Explain the process of photosynthesis as the ultimate Illustrated lectures

energy source.
9.2 Describe the nature of biomas i.e plant and animal “
biomass as sources of carbon for technological
processes.
9.3 Explain waste materials as substrate for “
biotechnological processes.
9.4 Identify the sources of biomass. “
9.5 Describe the processes involved in the conversion of “
biomas to useable fuels e.g combustion, chemical
processes aqueous processes etc.
98
WEEK General Objectives : 10.0 Know the application of biotechnology in agriculture and forestry.
11 - 12 10.1 Explain plant cell culture. Illustrated lectures Teaching tools

10.2 List the techniques used in plant cell culture. “ “
10.3 Describe the role of biotechnology in increasing the “ “
activities of nitrogen fixing micro organisms in
nitrogen fixation. “
10.4 Describe the production of microbial insecticides or “
entomopathogens (bacteria, fungi, viruses) for the
control of insect pests. “
10.5 Describe the importance of biotechnology in “
agricultural crop production. “
10.6 Describe the role of biotechnology in forestry “
industries.
99
WEEK General Objectives : 11.0 Understand the role of biotechnology in environmental Technologies.
11.1 Describe the methods of waste water and sewage Illustrated lecture Audio visuals, charts.
treatment.
11.2 Describe the roles of microbes as catalytic agents in “ “
geological processes e.g. mineral formation, mineral
degradation, sedimentation, weathering,
geochemical cycling. “
11.3 Explain the side effects of microbial involvement “
with minerals e.g. production of sulpheric acid;
production that causes pollution, microbial
weathering of limestone etc. “
11.4 List the beneficial effects of microbes in “
environmental technology. “
11.5 Explain waste materials as substrate for “
biotechnological processes. “
11.6 Identify the agricultural wastes/by-products that “
serve as substrate for biotechnological processes. “
11.7 Explain forestry wastes/by-products as substrate for “
biotechnological processes.
11.8 List industrial by-products/wastes that are substrates “
for biological processes.

5-6 Identify experimentally microorganism used in Conduct practical on Microscopes, culture media
biotechnological processes microorganism identification
for biotechnological processes
100
PROGRAMME: BIOCHEMISTRY HIGHER NATIONAL DIPOMA
COURSE: TISSUE BIOCHEMISTRY
CODE: STH 421
DURATION: 60Hours/ 14 Weeks Lecture=1 Tutorial=0 Practical=3
UNIT: 3.0
GOAL: This course is designed to provide diplomates with understanding of the
Biochemical functions of various tissues and membrane.
GENERAL OBJECTIVES: On completion of this course, diplomates should be able to:
1.0 Understand the structure and functions of biological membranes.
2.0 Understand the structure, functions and mode of action of excitable
membranes,tissues and sensory systems.
3.0 Know the biochemistry of muscle tissue and cell morality.
101
Course: Tissue Biochemistry Course Code: STH 421 Contact Hours: 60 Hours 1-0-3
Course Goal: This course is designed to provide with an understanding of the biochemical functions of various fuscous and
membrane.
WEEK General Objectives: 1.0 Understand the structure and functions of biological membranes.

1.1 Describe the structure of membrane as Explain the structure of
organized assembles constituting of proteins and membrane as a organized
lipids, that separate cells from the environment. assembles constituting protein
and lipids that separate cell
1.2 List the common features of biological from the environment.
membrane. Describe the common features
of biological membranes.
1.3 Explain phospholipids as the major class of Lecture and describe the
membrane lipids. phospholepid as a major class
of membrane lipids.
1.4 Explain the formation of bilayers by Describe the formation of
phospholipids and glycolipids. bilayers by phospholipids and
glycolipids.
1.5 Describe the structure of the lipids bilayer.
Lecture and discuss the
1.6 Explain that lipid bilayer are permeable to ions structure of bilayers.
and polar molecules. Discuss lipid layers
permeability to ions and polar
1.7 Explain the role of proteins in membrane molecules.
processes.
Specify the role of proteins in
1.8 Reconstituting functional membrane in the membrane processes.
laboratory.
102
1.9 Describe the nature of the membranes of
the red cell View cell Microscope
the mitochondrion
the plasma
1.10 Describe the fluid mosaic model of the
biological membrane.
1.11 Explain the features of membrane fluidity.
1.12 Explain the regulation of flow of ions and
molecules between cells by specific membrane
transport system.
1.13 Outline the roles of the transport processes.
1.14 Distinguish between active and positive
transport.
1.15 Explain the sodium-potassium pump.
1.16 Explain the role of Na+-K+ ATpase as an
integral part of the
sodium-potassium pump.
1.17 Describe the sodium-potassium as an
oligomeric trans-
membrane protein.
1.18 Describe a model for the mechanism of Na+-
K+ pump.
1.19 List the inhibitors of the Na+-k+ pump.
103
1.20 Explain the transportation of calcium by a
different Atpase.
1.21 Explain that active transport of sugar is
couple to their
phosphorylation.
1.22 Describe the ionophores
1.23 (transport anti-biotic).
1.24 Explain the functions of lonophores (transport Lecture and discuss the
anti-biotic). function of lonophores as a
1.25 Describe the methods of membrane isolation. transport antibiotics.
Explain the methods of
membrane isolation.
104
WEEK General Objectives: 2.0 Understand the Structure, functions and mode of action of excitable membranes, tissues and
sensory systems.
5 - 13 2.1 Distinguish between resting and action potentials in Illustrated lectures
nerve impulse transmission. “
2.2Explain that an action potential is generated when the
membrane potential is above the thresh value (i.e. from “
60 – 40 mV).
2.4 haism of a ction ptentials in membranes.
2.5 Describe the action of tetrad toxin and serotoxins “
(inhibitors).
2.6 Explain neurotransmitter. “
2.7 Classify neurotransmitter substances (e.g. excitable
and inhibitory). “
2.8 Describe acetylcholines as neurotransmitter. “
2.9 Explain how catescholamine and gamma-aminobuty
rate (GABA) are also neurotransmitters. “
2.10Describe the reactions at synaptic junctions. “
2.11Explain butrycholine as an anaesthetic agent.
2.12Define dibucaine number.
105
WEEK General Objectives: 2.0 Understand the Structure, functions and mode of action of excitable membranes, tissues and
sensory systems.
2.13List excitable receptors that are activated by light. “
2.14Describe the structure of the retinal rod cells. “
2.15Explain the effects of light on retinal rod cells.
2.16Explain the mode of action of the eye lens. “
2.17Explain the biochemistry of visual process. “
2.18Explain the causes of cataract and night blindness. “
2.18Explain the theories put forward to explain increased “
vision of some animals subdued light. “
106
WEEK General Objectives : 3.0 Know the biochemistry of Muscle tissue and cell mortality.
Biochemistry of muscle tissue

13 - 14 3.1 Describe the conversion of chemical energy to
mechanical energy in the muscle. Illustrated lectures
3.2 Identify the different types of muscles.
3.3 Describe the nature and structure of the muscle Practical identification in the
protein e.g. myoglobin. laboratory.
3.4 Describe the interaction of thick and thin filaments of Drawings
the muscle. Illustrated lectures
3.5 Describe the nature and structure of the thick and thin
filaments. Drawings
3.6 Describe the structure of myosin content of the thick
filament. “
3.7 Explain the role of action in ATP age activity.
3.8 Explain with the aid of a diagram the functions of “
actin and myosin. “
3.9 Explain the molecular basis of muscle contraction.
3.10Explain the sources of energy for muscle contraction. Illustrations
3.11Describe phosphocreatine as a reservoir of phosphate “
bond. “
3.12Describe muscle as a thermodynamic machine.
3.13Explain the role of glucose, fatty acids and ketone “
bodies as major fuels for the muscle. “
3.14Explain muscle as the major stone of glycogen.
3.15Determine the glucose level in the blood and urine. “
Lab. Experiment on the glucose.
107
WEEK General Objectives: 3.0 Contd.
13 - 14 3.13 Explain the role of glucose, fatty acids and ketone Illustrations
bodies as major fuels for the muscle.
3.14 Explain muscle as the major store of glycogen. “
3.15 Determine the glucose level in the blood and urine. Laboratory experiment on the
3.16 Explain the role of muscle in a storing organism. glucose.
3.17 Estimate glucose level in a fasting and fed state.
WEEK PRACTICALS TEACHEARS ACTIVITIES RESOURCES

13-14 3.14 Determine experimentally the glucose Laboratory experiment of Sample of blood urine
level in the blood urine glucose level in blood urine
108
PROGRAMME BIOCHEMISTRY HIGER NATIONAL DIPLOMA
COURSE FORENSIC BIOCHEMISTRY
CODE STH 422
DURATION 45 hours/14 weeks/lecture = 1 Tutorial =0 Practical = 2
UNIT 2.0
GOAL This course is designed to provide diplomatses with basic
knowledge of biochemistry in a forensic science
laboratory.
GENERAL OBJECTIVES:
On completion of this course, diplomate should be able to:
1.0 Understand the metabolism of foreign compounds (Xenobiotics) antibody
2.0 Understand analysis of materials of forensic interest.
109
Course: Forensic Biochemistry Course Code: STH 422 Contact Hours: 45 Hours 1-0-3
Course Goal: This course is designed to provide students with basic knowledge of the application of
biochemistry in a forensics science laboratory.
WEEK General Objectives: 1.0 Understand the metabolism of foreign compounds (Xenobiotics)
antibody.
1–4 Special Learning Objective: Teachers Activities Resources
110
Metabolism of foreign compounds in the Illustrative lectures. Teaching tools.
blood.
“
1.1 Describe drugs as foreign chemical “
compounds in the system. “
1.2 Classify drugs as acidic, basic and neutral. “
1.3 Explain the role of the liver enzymes in
foreign compound metabolism. “
1.4 Describe the characteristics of foreign “
compound metabolizing enzymes.
1.5 Explain the role of the smooth Endoplasmic “
recticulum in foreign compound metabolism. “
1.6 Explain the two phases in the metabolism of
foreign compounds (phase I and II). “
1.7 Explain phase I as involving the modification “
of the drug via oxidation and reduction
reactions.
“
111
1.8 Explain Phase II as dealing with the Illustrative lectures. Teaching tools.
conjugation of Phase I products mainly into
water extractable produce e.g. glucoronides, “
sulphases. Etc. “
1.9 Explain how metabolism of a drug may “
enhance or lower the harmful effect of a drug “
or make an in nocons compound harmful.
1.10 Explain how the effect (metabolism) of a “
drug in the system depends on such factors as “
the structure of the compound route of
administration, sex and strain and species of “
animal, presence of other chemicals, diet etc. “
1.11 compound harmful.
1.12 Explain how the effect (metabolism) of a Audio visual
drug in the system depends on such factors as
administration, sex and strain and species of
animal, presence of other chemicals, diet etc.
1.13 compound harmful.
1.14 Explain how the effect (metabolism) of a
drug in the system depends on such factors as
administration, sex and strain and species of
animal, presence of other chemicals, diet etc.
1.15 Explain the terms: toxicity, carcinogen
city, mutagenicity detragenicity etc.
112
WEEK General Objectives : 1.0 Understand the metabolism of foreign compounds (xenobiotics) antibody.
5-7 Special Learning Objective: Teachers Activities Resources
1.16 Explain the effects of drugs on tissues in terms of 1.11 Illustrate lecture Teaching tools
above.
1.17 Describe the various routes of excretion of drugs and their “ “
metabolites (breakdown produces) e.g exhaled air, sweat, “
saliva, urine, bile and other body fluids.
1.18 Explain the importance of the study of rate of urinary “ “
excretion of drugs in forensic science. Urine analysis on drug
1.19 Explain the importance of the study of rate of urinary administration.
excretion of drugs in forensic science. Practical extraction.
1.20 Explain drug-drug interactions in the body. Food test.
1.21 Extract drugs from biological tissues. “
1.22 Monitor contaminants in foods and beverages. Carry out analysis of drugs
1.23 Identify drugs using TLC, U.V. & I.R. spectroscopy. using TLC, UV, and IR.
1.24 Type blood stains and other blood stains. Carry out analysis on blood
1.25 Carry out test on blood stains l(dried and fresh). group,
“
113
Course: Course Code: Contact Hours
WEEK General Objectives:2.0Understand Analysis of Materials of forensic interest.

8-9 Materials of Forensic interest Illustrate lectures. Teaching tools.
2.1 Explain forensic science. “ “
2.2 Describe the collection , preservation and
forwarding of materials of forensic interest to the
laboratory. “
2.3 Explain the need for proper storage of materials “
for forensic analysis.
2.4 Explain the importance of preserving some “
portions of a sample for further reference. “
2.5 Describe the duties of the toxicologist.
2.6 Describe the various groups of poisons.
2.7 Explain the methods of extraction and “ “
identification of compounds of forensic interest.
2.8 Describe the extraction and identification of
poison and drugs.
2.9 Explain metallic poisoning, indicating where
they are deposited in the body.
Extract poison from a formulated sample
WEEK General Objectives : 1.0 Understand the metabolism of foreign compounds (xenobiotics) antibody.
Special Learning Objective: Teachers/Learning Resources
Activities
10 - 11 2.10Describe the methods of extraction and specific Illustrative lecture.
identification of 2.9 above. Practical spot tests on
2.11Describe blood groups and rhesin factors. metallic poisoning.
2.12Carryout blood group typing tests, explain blood Practical blood group test.
group typing.
114
WEEK General Objectives : 2.0 Contd.
12 - 14 Special Learning Objective: Teachers/Learning Activities Resources
2.13Explain parentage dispute. Illustrative lecture
2.14Describe the use of blood group in 2.13 above. “ Teaching tools
2.15Describe the various types of body fluids. Urine analysis on drug
2.16Describe qualitative methods of identification of administration “
blood strains, urine and saliva. Practical extraction.
2.17Describe various presumptive (preliminary) tests
employed on body fluids (e.g. blood; saliva, semon) “
before specific conformatory tests.
2.18Explain species identification for blood strain.
2.19Carry out test on blood stains, saliva, smina stains Carry out analysis on saliva.
and species identification.
2.20Define hard drugs. “
2.21Classify hard drugs.
2.22Describe spot test for drugs of forensic interest.
2.23Describe methods of purification of of such hard
drugs.
2.24Describe standard confirmatory methods of analysis “
of hard drugs.
2.25Carry out qualitative test on different drugs.
115
WEEK General Objectives : 2.0 Contd.
2.26Compare results obtained in 2.23 above with the Illustrative lecture
normal level (data) set by Nigerian standards Teaching tools
organization, food and Drug administration (FDA)
and World Health Organization (WHO) and similar “
bodies.
2.27Make proper deductions from all available data. “
2.28Build up result/data banks for future references. “ “
2.29Explain presentation pattern of work reports. “
2.30Explain why the analyst must report only his
findings.

8-9 2.19 Carry out blood stains Saliva and simian Carry out analysis on saliva Saliva
stain and species identification
2.25 Carry out qualitative test on different Conduct qualitative test on Drug sample
12-14 drugs drugs
116
COURSE: INDUSTRIAL BIOCHEMISTRY
CODE: STH 423
DURATION: 60Hours/14Weeks/Lecture = 1 Tutorial = 0 Practicals = 3
UNIT: 3.0
GOAL: This course is designed to provide the diplomate with understanding of industrial
Function of biochemist of industry process.
GENERAL OBJECTIVE:
On completion of this course, diplomate should be able to :
Understand mode of action of pesticides resides on tissues and there regarding product
Know general method of isolation and identification of drugs an tissues
Know methods of water analysis treatment and assessment of purity.
Know food toxins then elimination from food tissues.
Understanding the chemical and enzymatic principle of starch conversion and its
Industrial application.
Understanding the chemical and enzymatic principles of starch conversion and it
Industrial application the quality control methods in the industry.
Understand
Understand general methods of preservation process in food industry.
117
Course: Industrial Biochemistry Course Code: STH 423 Contact Hours 60 Hours 1-0-3
Goal: This course is designed to provide the student with an understanding industrial function of biochemist of
industry process.
WEEK General Objectives: Understand mode of action of Pesticides residues on tissue and their degradation
product.
1–2 Special Learning Objective: Teachers Activities Resources
Pesticides Lecture. Lecture.
1.1 Explain the term “pesticides”. “ “
1.2 List types of pesticides and their chemical structures.
1.3 Describe the biochemical actions of pesticide. “ “
1.4 Illustrate with chemical are actionsthe degradative
products of pesticides in the system. “ “
1.5 Describe the biochemical effects of pesticide residues
on soil, plant and man.
1.6 Identify and quantify the residues isolated in 1.6
above. “ “
1.7 Compare residues isolated in 1.6 above with control
levels set by Nigeria Standard Organisation and food
and Drugs Administration. “ “
1.8 Test effects of pesticides on annual tissues.
118
WEEK General Objectives : 2.0 Know General methods of
isolation and identification of drug and tissue.
2.1 Describe types of drugs as acidic, basic or neutral. Lecture.
2.2 Extract drugs from body fluids and tissues. Demonstrate experiment on
2.3 Identify and quantify the extracts in 2.2 above. drug analysis.
2.4 State the optional conditions of extraction. Lecture. Drug, animal tissues.
2.5 Test effect of drugs on annual tissues. Demonstrate experiment, the
effect of drug on animal
tissues.
119
WEEK General Objectives : 3.0 Know methods of water analysis treatment and assessment of purity.
Special Learning Objective: Teachers Resources

3-4
ivities
3.1 Describe chemical and physical methods of water Lecture. Visit the water works co-
analysis for the following constituents, PH, total operation.
solid, hardness, chlorides, carbonates, sulphates,
lodides, fluorides, nitrates, dissolved oxygen, iron,
lead etc.
3.2 Compare data on water samples with acceptable Demonstrate practical on water.
standards. Samples.
3.3 Describe methods of reducing the constituents in Lecture.
3.2. above to acceptable levels. Lecture.
3.4 Describe other methods of water treatment e.g.
filtration, distillation, sedimentation etc. Demonstrate practical on
3.5 Treat impure water to purity by known methods of separation methods.
water treatment.
120
WEEK General Objectives : 4.0 Know food toxins and their elimination from food tissues.
5-6 4.1 List types of food toxins. Lecture. Visit to the medical
4.2 Describe the biochemical mode of action of toxin. Lecture. laboratory technology
4.3 Describe chemical and biochemical methods of isolation and Lecture. section of hospitals.
identification of toxins. Demonstrate Practical on Isolation
4.4 Isolate and identify toxins (exo and endo). and Identification of toxics.
4.5 Compare the levels of toxins with those reported by experts in
the field.
4.6 Describe “inoitio” or biochemical mechanisms of detoxification
e.g hydrolysis, oxidation, reduction, conjugation etc.
4.7 Explain the role of the liver in detoxification.
4.8 Explain how toxic substances and their products are eliminated
after detoxification by the liver through expired air and body Lecture.
fluids.
Explain how toxic substances and their products are eliminated after
detoxification by the liver through expired air and body fluids.
Lecture.
121
WEEK General Objectives: 5.0 Understand the chemical and enzymatic principles of starch conversion and it industrial application.
7-8 5.1 Describe the chemical structure and rheological properties of starch. Lecture. Visit to the breweries
5.2 Describe enzymatic degradation of starch and starch base products. industry.
5.3 List the industrial applications of starch as raw materials.
5.4 Explain how configuration and conformational state of hydrolytic product “
of starch govern their industrial uses.
5.5 Explain starch quality in terms of their binding characteristics and
amylose/amylopectin ratio. “
5.6 List products that potentially can be prepared from starch after enzymatic
degration e.g low dextrose syrups, high maltose syrups. “
5.7 Describe polymerization and depolymerisation of starch and industrial
applications.
5.8 Describe enzymatic isomerisation of corn-based syrups and their
application. “
5.9 Explain the chemical principles involved in reproduction of starch-based
glucose syrups and products.
5.10Produce starch based glucose syrup.
5.11Determine experimentally the quality and rheology of starch (e.g cassava, “
yam, guinea corn etc).
122
WEEK General Objectives: 6.0 Understand the chemical and enzymatic principles of starch conversion and it industrial application.
9 - 10 6.1 Define the term fermentation. Lecture.
6.2 Explain the biochemistry of fermentation. “ Visit to breweries.
6.3 Describe limited and complete fermentation reactions and their industrial
applications. “
6.4 Describe commercial (enzyme/yeast) extraction, purification, storage and
recovery.
6.5 State the advantage of storage of yeast in the dry form. “
6.6 Describe fermentation process in alcohol industry.
6.7 Describe alcoholic fermentation as similar to glycolysis pathway but
requires two different enzymatic steps at the end. “
6.8 List products of industrial fermentation.
6.9 List products of local fermentation. Demonstration experimentally.
6.10 Outline the processes of production of Beer (top and bottom), wine, Fermentation reaction.
yeast.
6.11 Describe the role of fermentation in the production of garri, fermented Lecture.
oil bean, palm wine, burukutu.
123
WEEK General Objectives : 7.0 Understand the quality control methods in the industry.
Special Learning Objectives Teachers Activities Resources
11 - 12 7.1 Explain sampling procedure e.g. in food, alcohol and drug. Lecture Visit to the food industry.
7.2 Apply biochemical techniques in quality control.
7.3 Analyze by standard methods (both raw and finished products) “
such constituents as humidity, free and bound water, ash, fibre
content, trace elements etc. “
7.4 Estimate protein content by kjeldahl method and formal
titration.
7.5 Determine carbohydrate, lipid and vitamin contents of various
food and beverage items. Kjeldahl apparatus.
7.6 Estimate drugs composition. Demonstrate the use of
7.7 Interpret the significance of results obtained from analyses in Kjeldahl apparatus in
7.2 to 7.6 above. determine protein content.
7.8 Deduce from the results in 7.2 to 7.6 above whether or not they Experiment of drug
meet set standards. composition.
124
WEEK General Objectives : 8.0 Understand general methods of Preservation Processes in food Industry.
Special Learning Objectives Teachers Activities Resources
13 - 14 8.1 Explain the term “preservation”. Lecture.

8.2 State preservation methods in food industry. “
8.3 Explain the principles of physical and chemical methods of
preservation. “
8.4 Describe the side effects of chemical and physical methods of
preservation of foods.
8.5 Describe the biochemical effects of preservatives on the “
tissues and organs.

1-2 1.8 Test effects on pesticide on annual tissues Conduct test on the effect of Pesticide and annual tissues
pesticide on annual tissues
3-4 3.2 Compare data on water samples with acceptable

standards
3.5 Treat in pure water to purity by knowing method
of water treatment
125
5-6 3.6 Isolate and identify toxins (Eco and Endo)
7-8 Determine experimentally the quality and rhea logy Demonstrate practical on Sample of starch
of starch (eg cassava, yam, guinea corn etc) quality and theology of starch
7.5 Determine carbohydrate, lipideral vitamins Conduct practical to detects the Drug sample
contents of various food and beverage items contents of carbohydrate, lipid
etc using procreate
7.6 Estimate drug composition Equipment of drug composition
126
LIST OF BIOCHEMISTRY EQUIPMENT
S/NO ITEMS QUANTITY

1 Balances 10
2 Asbestos sheets 50
3 Barometer 2
4 Beehive shelf 6
5 Blowpipe, nickel plated brass 20
6 Test-tube brush 30
7 Centrifuge 2
8 Buster brush 20
9 Bunsen burners 30
10 First aid cabinet 2
11 Clamp for retort stand, die cast aluminum 30
12 Clip, Hofmann’s screw 40
13 Combustion boat, porcelain 40
14 Distillation apparatus 5
15 Crucible purcelian with lid 40
16 Electrode, carbon plate with terminal 6
17 Filter pump, nickel plate brass 2
18 Fume boards 2
19 Gauge with ceramic centre 40
20 Gloves, (asbestos and rubber) 10
21 Holder for test tubes 30
22 Kipp’s apparatus 1
23 Mortar and pestle 4
24 Oven electric, thermostatic control 1
25 Porous pot 3
26 Printer, tape 2
27 Vacuum pump 1
28 Rack for flasks and test tubes 20 each
29 Rule, I meter 2
127
30 Khjeldal apparatus 5
31 Spatula 2
32 Polytechnic spheres for modals 20
33 Sphints, wooden 50
34 Retort stand with rod 5 bundles
35 Steam generator 20
36 Steam trap(all glass) 2
37 Magnetic stirrer 2
38 Thermometers 4
39 Tongs 20
40 Tripad 40
41 Voltammeter 2
42 Water bath with rings 4
43 Water still manesty 1
44 Refratometer 1
45 Weighting bottles 20
46 Heating mantle 4
47 Hotplate 4
48 Plastic aspirator 4
49 PH meter 4
50 Portable autoclave 2
51 Muffie furnance 2
52 Thermostated water bath 2
53 Mahler-Cook bump calorimeter 2
54 Vacuum dry oven 1
55 Water deionsar 2
56 Conductivity meter 1
57 Acid shower 1
58 Spectrephezometer-(UV) 2
59 Melting point apparatus 2
60 Wrist type flask shaker 3
61 Soxhlet extraction apparatus 2
128
62 Colorimeter visual photoelectric 1
63 Flame photometer 1
64 Polarimeter 2
65 Chromatography kits-paper/TLC with spreader for TLC 1
66 Electrophoresis equipment 2
67 Store 1
68 Preparatory room 2
129
LIST OF PARTICIPANTS
S/NO NAMES ADDRESS

1 Bikomo, E.O. (PRS) Chemistry science department
Yaba College of Technology
Yaba, Lagos
2 Asaolu .O. (Mrs) Department of science Laboratory
Technology,
The Polytechnic, Ibadan
3 Adeyemi, H. Yemi Department of Science Laboratory
Technology
Federal Polytechnic, Bida
4 Mrs. Ibrahim H. Science Laboratory Technology
department
Federal Polytechnic, Offa
5 Ogugua E. Okafo National Board for Technical Education.
6 Mrs. Stella Adetola National Board for Technical Education
130

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NATIONAL BOARD FOR TECHNCIAL EDUCATION

HIGHER NATIONAL DIPLOMA

CURRICULUM AND COURSE SPECIFICATIONS

PLOT ‘B’ BIDA ROAD, P.M.B. 2239, KADUNA-NIGERIA

STRUCTURE OF THE PROGRAMME:

NATIONAL DIPLOMA (ND)

HIGHER NATIONAL DIPLOMA

GUIDANCE NOTE FOR TEACHERS TEACHING THE PROGRAMME

GUIDANCE FOR THE SIWES PROGRAMME

Responsibility for Placement of Students

Evaluation of Students during the SIWES

THE INSTITUTION BASED SUPERVISOR

STIPEND FOR STUDENTSS IN SIWES

SIWES as a Component of the Curriculum

National Board for Technical Education,

GLT Course see General Laboratory Techniques syllabus

COURSE COURSE TITLE L T P CU CH PRE-REQUISITE

COURSE COURSE TITLE L T P CU CH PRE-REQUISITE

3-5 2.1 Define Centrifugation Lecture Teaching tools

6-7 3.1 Explain the term “dialysis” Lecture

WEEK PRACTICALS TEACHERS ACTIVITIES RESKOURCES

Interpret the results obtain in 5.11

6.2 Analyse the method of

Guide students to analyse lip cal Abbe refmetometer

WEEK PRACTICAL TEACHERS ACTISITIES RESOURCES

1.19Determine osmotic pressure of a solute

Special Learning Objective: Teachers Activities Resources

WEEK PRACTICAL STEACHERS ACTIVITIES RESOURCES

5.6 Carry out any of the following Conduct practical on Reagents

Special Learning Objective: Teachers Activities Resources

WEK PRACTICALS TEACHERS ACTIVITIES RESOURCES

Special Learning Objectives: Teachers/Learning Activities Resources

Special Learning Objective: Teachers/Learning Activities

2.43Describe the uses of isoenzymes in biological Lecture

WEEK PRACTICAL TEACHERS ACTIVITIES RESOURCES

1-2 1.0 Understand electrophoresis as a method of Carry out experiment on

Special Learning Objective: Teachers/Learning Activities

WEEK General Objectives : 2.0 Understand the Principle of Spectrophotometry

2.1- Explain the electromagnetic emission spectrum. Demonstrate the spectrum.

WEEK General Objectives : 2.0 Understand the Principle of Spectrophotometry

Practical sample analysis. “

Special Learning Objective: Resources

WEEK General Objectives : 4.0 Understand the Principle of Spectrophotometry

Special Learning Objective: Resources

Special Learning Objective: Teachers/Learning Activities Resources

3.7 Prepare sample for analysis by Practicals on sample Spectroflorimeter

Special Learning Objective: Teachers Activities Resources

Special Learning Objective: TeachersActivities

Special Learning Objective: Teachers Activities Resources

Special Learning Objective: Teachers Activities

Special Learning Objective: TeachersActivities Resources

4-6 Special Learning Objective: Teachers Activities

10 - 12 Special Learning Objective: Teachers/Learning Activities

Special Learning Objective: Teachers/Learning Activities

3.20 Isolate and separate nucleic acid Practical isolation and

3.21 Measure and identify nucleic acid Practical measurement of

Special Learning Objective: Teaching Activities Resources

Special Learning Objective: Teachers Activities Resources